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Volumn 1, Issue , 2008, Pages 247-313

Stability and Design of α-Helices

Author keywords

Design; Ligands; Polypeptide chain; Residues; Schellman motif

Indexed keywords


EID: 84889766283     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527619498.ch9     Document Type: Chapter
Times cited : (17)

References (303)
  • 1
    • 76549252207 scopus 로고
    • The structure of proteins: two hydrogen-bonded helical configurations of the polypeptide chain
    • Pauling, L., Corey, R. B., and Branson, H. R. (1951). The structure of proteins: two hydrogen-bonded helical configurations of the polypeptide chain. Proc. Natl Acad. Sci. USA 37, 205-211.
    • (1951) Proc. Natl Acad. Sci. USA , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 2
    • 0000591348 scopus 로고
    • New X-ray evidence on the configuration of polypeptide chains
    • Perutz, M. F. (1951). New X-ray evidence on the configuration of polypeptide chains. Nature 167, 1053-1054.
    • (1951) Nature , vol.167 , pp. 1053-1054
    • Perutz, M.F.1
  • 4
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow, D. J. and Thornton, J. M. (1988). Helix geometry in proteins. J. Mol. Biol. 201, 601-19.
    • (1988) J. Mol. Biol. , vol.201 , pp. 601-619
    • Barlow, D.J.1    Thornton, J.M.2
  • 6
    • 0029028490 scopus 로고
    • A-helix formation by peptides of defined sequence
    • Baldwin, R. L. (1995). a-helix formation by peptides of defined sequence. Biophys. Chem. 55, 127-35.
    • (1995) Biophys. Chem. , vol.55 , pp. 127-135
    • Baldwin, R.L.1
  • 8
    • 0002889181 scopus 로고    scopus 로고
    • CD spectroscopy and the helix-coil transition in peptides and polypeptides
    • In Circular Dichroism and the Conformational Analysis of Biomolecules G. D. Fasman, editor, Plenum Press, New York
    • Kallenbach, N. R., Lyu, P., and Zhou, H. (1996). CD spectroscopy and the helix-coil transition in peptides and polypeptides. In Circular Dichroism and the Conformational Analysis of Biomolecules G. D. Fasman, editor, Plenum Press, New York, 201-59.
    • (1996) , pp. 201-259
    • Kallenbach, N.R.1    Lyu, P.2    Zhou, H.3
  • 9
    • 0032317156 scopus 로고    scopus 로고
    • Deciphering rules of helix stability in peptides
    • Rohl, C. A. and Baldwin, R. L. (1998). Deciphering rules of helix stability in peptides. Meth. Enzymol. 295, 1-26.
    • (1998) Meth. Enzymol. , vol.295 , pp. 1-26
    • Rohl, C.A.1    Baldwin, R.L.2
  • 10
    • 0033215173 scopus 로고    scopus 로고
    • Forming stable helical peptides using natural and artificial amino acids
    • Andrews, M. J. I. and Tabor, A. B. (1999). Forming stable helical peptides using natural and artificial amino acids. Tetrahedron 55, 11711-43.
    • (1999) Tetrahedron , vol.55 , pp. 11711-11743
    • Andrews, M.J.I.1    Tabor, A.B.2
  • 11
    • 0034581611 scopus 로고    scopus 로고
    • The relationship between sequence and structure in elementary folding units
    • Serrano, L. (2000). The relationship between sequence and structure in elementary folding units. Adv. Protein Chem. 53, 49-85.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 49-85
    • Serrano, L.1
  • 12
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of a helices
    • Richardson, J. S. and Richardson, D. C. (1988). Amino acid preferences for specific locations at the ends of a helices. Science 240, 1648-52.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 13
    • 0024290488 scopus 로고
    • Helix signals in proteins
    • Presta, L. G. and Rose, G. D. (1988). Helix signals in proteins. Science 240, 1632-41.
    • (1988) Science , vol.240 , pp. 1632-1641
    • Presta, L.G.1    Rose, G.D.2
  • 15
    • 0023521842 scopus 로고
    • Analysis of the relationship between side-chain conformation and secondary structure in globular proteins
    • MacGregor, M. J., Islam, S. A., and Sternberg, M. J. E. (1987). Analysis of the relationship between side-chain conformation and secondary structure in globular proteins. J. Mol. Biol. 198, 295-310.
    • (1987) J. Mol. Biol. , vol.198 , pp. 295-310
    • MacGregor, M.J.1    Islam, S.A.2    Sternberg, M.J.E.3
  • 16
    • 0029147823 scopus 로고
    • Intrinsic f;c propensities of amino acids derived from the coil regions of known structures
    • Swindells, M. B., MacArthur, M. W., and Thornton, J. M. (1995). Intrinsic f;c propensities of amino acids derived from the coil regions of known structures. Nat. Struct. Biol. 2, 596-603.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 596-603
    • Swindells, M.B.1    MacArthur, M.W.2    Thornton, J.M.3
  • 17
    • 0028429178 scopus 로고
    • Conformational analysis of the backbone-dependent rotamer preferences of protein side-chains
    • Dunbrack, R. and Karplus, M. (1994). Conformational analysis of the backbone-dependent rotamer preferences of protein side-chains. Nat. Struct. Biol. 1, 334-9.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 334-339
    • Dunbrack, R.1    Karplus, M.2
  • 18
    • 0036667731 scopus 로고    scopus 로고
    • Rotamer libraries in the 21(st) century
    • Dunbrack, R. L. (2002). Rotamer libraries in the 21(st) century. Curr. Opin. Struct. Biol. 12, 431-40.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 431-440
    • Dunbrack, R.L.1
  • 19
    • 0033582944 scopus 로고    scopus 로고
    • Side-chain structures in the first turn of the a-helix
    • Penel, S., Hughes, E., and Doig, A. J. (1999). Side-chain structures in the first turn of the a-helix. J. Mol. Biol. 287, 127-43.
    • (1999) J. Mol. Biol. , vol.287 , pp. 127-143
    • Penel, S.1    Hughes, E.2    Doig, A.J.3
  • 20
    • 0024972479 scopus 로고
    • Capping and a-helix stability
    • Serrano, L. and Fersht, A. R. (1989). Capping and a-helix stability. Nature 342, 296-9.
    • (1989) Nature , vol.342 , pp. 296-299
    • Serrano, L.1    Fersht, A.R.2
  • 21
    • 0026696173 scopus 로고
    • Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59
    • Bell, J. A., Becktel, W. J., Sauer, U., Baase, W. A., and Matthews, B. W. (1992). Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. Biochemistry 31, 3590-6.
    • (1992) Biochemistry , vol.31 , pp. 3590-3596
    • Bell, J.A.1    Becktel, W.J.2    Sauer, U.3    Baase, W.A.4    Matthews, B.W.5
  • 22
    • 0027367977 scopus 로고
    • Helix capping propensities in peptides parallel those in proteins
    • Chakrabartty, A., Doig, A. J., and Baldwin, R. L. (1993). Helix capping propensities in peptides parallel those in proteins. Proc. Natl Acad. Sci. USA 90, 11332-6.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11332-11336
    • Chakrabartty, A.1    Doig, A.J.2    Baldwin, R.L.3
  • 23
    • 0027404071 scopus 로고
    • Stabilization of a-helical structures in short peptides via end capping
    • Forood, B., Feliciano, E. J., and Nambiar, K. P. (1993). Stabilization of a-helical structures in short peptides via end capping. Proc. Natl Acad. Sci. USA 90, 838-42.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 838-842
    • Forood, B.1    Feliciano, E.J.2    Nambiar, K.P.3
  • 24
    • 0027212028 scopus 로고
    • Design of helix ends. Amino acid preferences, hydrogen bonding and electrostatic interactions
    • Dasgupta, S. and Bell, J. A. (1993). Design of helix ends. Amino acid preferences, hydrogen bonding and electrostatic interactions. Int. J. Pept. Protein Res. 41, 499-511.
    • (1993) Int. J. Pept. Protein Res. , vol.41 , pp. 499-511
    • Dasgupta, S.1    Bell, J.A.2
  • 25
    • 0027204024 scopus 로고
    • Helix stop signals in proteins and peptides: the capping box
    • Harper, E. T. and Rose, G. D. (1993). Helix stop signals in proteins and peptides: the capping box. Biochemistry 32, 7605-9.
    • (1993) Biochemistry , vol.32 , pp. 7605-7609
    • Harper, E.T.1    Rose, G.D.2
  • 26
    • 0027986703 scopus 로고
    • Sequence determinants of the capping box, a stabilizing motif at the N-termini of ahelices
    • Seale, J. W., Srinivasan, R., and Rose, G. D. (1994). Sequence determinants of the capping box, a stabilizing motif at the N-termini of ahelices. Protein Sci. 3, 1741-5.
    • (1994) Protein Sci. , vol.3 , pp. 1741-1745
    • Seale, J.W.1    Srinivasan, R.2    Rose, G.D.3
  • 27
    • 0029009067 scopus 로고
    • The hydrophobic-staple motif and a role for loop residues in a-helix stability and protein folding
    • Muñoz, V. and Serrano, L. (1995). The hydrophobic-staple motif and a role for loop residues in a-helix stability and protein folding. Nat. Struct. Biol. 2, 380-385.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 380-385
    • Muñoz, V.1    Serrano, L.2
  • 28
    • 0032846342 scopus 로고    scopus 로고
    • Stable proline box motif at the N-terminal end of a-helices
    • Viguera, A. R. and Serrano, L. (1999). Stable proline box motif at the N-terminal end of a-helices. Protein Sci. 8, 1733-42.
    • (1999) Protein Sci. , vol.8 , pp. 1733-1742
    • Viguera, A.R.1    Serrano, L.2
  • 29
    • 0029020484 scopus 로고
    • N-and C-capping preferences for all 20 amino acids in a-helical peptides
    • Doig, A. J. and Baldwin, R. L. (1995). N-and C-capping preferences for all 20 amino acids in a-helical peptides. Protein Sci. 4, 1325-36.
    • (1995) Protein Sci. , vol.4 , pp. 1325-1336
    • Doig, A.J.1    Baldwin, R.L.2
  • 30
    • 0030447864 scopus 로고    scopus 로고
    • Helix propagation and N-cap propensities of the amino acids measured in alaninebased peptides in 40 volume percent trifluoroethanol
    • Rohl, C. A., Chakrabartty, A., and Baldwin, R. L. (1996). Helix propagation and N-cap propensities of the amino acids measured in alaninebased peptides in 40 volume percent trifluoroethanol. Protein Sci. 5, 2623-37.
    • (1996) Protein Sci. , vol.5 , pp. 2623-2637
    • Rohl, C.A.1    Chakrabartty, A.2    Baldwin, R.L.3
  • 31
    • 0001428018 scopus 로고
    • The aL conformation at the ends of helices
    • Protein Folding
    • Schellman, C. (1980). The aL conformation at the ends of helices. Protein Folding 53-61.
    • (1980) , pp. 53-61
    • Schellman, C.1
  • 32
    • 0028173780 scopus 로고
    • Rules for a-helix termination by glycine
    • Aurora, R., Srinivasan, R., and Rose, G. D. (1994). Rules for a-helix termination by glycine. Science 264, 1126-30.
    • (1994) Science , vol.264 , pp. 1126-1130
    • Aurora, R.1    Srinivasan, R.2    Rose, G.D.3
  • 34
    • 0030691777 scopus 로고    scopus 로고
    • C-capping and helix stability: the Pro C-capping motif
    • Prieto, J. and Serrano, L. (1997). C-capping and helix stability: the Pro C-capping motif. J. Mol. Biol. 274, 276-88.
    • (1997) J. Mol. Biol. , vol.274 , pp. 276-288
    • Prieto, J.1    Serrano, L.2
  • 36
    • 0028330140 scopus 로고
    • Characterisation of interactions and metal-ion bindingsites in proteins
    • Jernigan, R., Raghunathan, G., and Bahar, I. (1994). Characterisation of interactions and metal-ion bindingsites in proteins. Curr. Opin. Struct. Biol. 4, 256-63.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 256-263
    • Jernigan, R.1    Raghunathan, G.2    Bahar, I.3
  • 37
    • 0032464349 scopus 로고    scopus 로고
    • Analyisis of zinc binding sites in protein crystal structures
    • Alberts, I. L., Nadassy, K., and Wodak, S. J. (1998). Analyisis of zinc binding sites in protein crystal structures. Protein Sci. 7, 1700-16.
    • (1998) Protein Sci. , vol.7 , pp. 1700-1716
    • Alberts, I.L.1    Nadassy, K.2    Wodak, S.J.3
  • 38
    • 11944257538 scopus 로고
    • Secondary structure nucleation in peptides-transition-metal ion stabilized a-helices
    • Ghadiri, M. R. and Choi, C. (1990). Secondary structure nucleation in peptides-transition-metal ion stabilized a-helices. J. Am. Chem. Soc. 112, 1630-2.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 1630-1632
    • Ghadiri, M.R.1    Choi, C.2
  • 39
    • 0037207106 scopus 로고    scopus 로고
    • Induction of helical structure in a heptapeptide with a metal cross-link: Modification of the Lifson-Roig Helix-Coil theory to account for covalent cross-links
    • Kise, K. J. and Bowler, B. E. (2002). Induction of helical structure in a heptapeptide with a metal cross-link: Modification of the Lifson-Roig Helix-Coil theory to account for covalent cross-links. Biochemistry 41, 15826-37.
    • (2002) Biochemistry , vol.41 , pp. 15826-15837
    • Kise, K.J.1    Bowler, B.E.2
  • 40
    • 0025675385 scopus 로고
    • Metal ion enhanced helicity in synthetic peptides containing unnatural, metal-ligating residues
    • Ruan, F., Chen, Y., and Hopkins, P. B. (1990). Metal ion enhanced helicity in synthetic peptides containing unnatural, metal-ligating residues. J. Am. Chem. Soc. 112, 9403-4.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9403-9404
    • Ruan, F.1    Chen, Y.2    Hopkins, P.B.3
  • 41
    • 0037433511 scopus 로고    scopus 로고
    • Effects of As(III) binding on a-helical structure
    • Cline, D. J., Thorpe, C., and Schneider, J. P. (2003). Effects of As(III) binding on a-helical structure. J. Am. Chem. Soc. 125, 2923-9.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2923-2929
    • Cline, D.J.1    Thorpe, C.2    Schneider, J.P.3
  • 42
    • 0027066845 scopus 로고
    • Differences in the amino acid distributions of 310-helices and a-helices
    • Karpen, M. E., De Haset, P. L., and Neet, K. E. (1992). Differences in the amino acid distributions of 310-helices and a-helices. Protein Sci. 1, 1333-42.
    • (1992) Protein Sci. , vol.1 , pp. 1333-1342
    • Karpen, M.E.1    De Haset, P.L.2    Neet, K.E.3
  • 44
    • 0014213849 scopus 로고
    • A second right-handed helical structure with the parameters of the Pauling-Corey a-helix
    • Némethy, G., Phillips, D. C., Leach, S. J., and Scheraga, H. A. (1967). A second right-handed helical structure with the parameters of the Pauling-Corey a-helix. Nature 214, 363-5.
    • (1967) Nature , vol.214 , pp. 363-365
    • Némethy, G.1    Phillips, D.C.2    Leach, S.J.3    Scheraga, H.A.4
  • 45
    • 0028921182 scopus 로고
    • Views of helical peptides-a proposal for the position of 310-helix along the thermodynamic folding pathway
    • Millhauser, G. L. (1995). Views of helical peptides-a proposal for the position of 310-helix along the thermodynamic folding pathway. Biochemistry 34, 3872-7.
    • (1995) Biochemistry , vol.34 , pp. 3872-3877
    • Millhauser, G.L.1
  • 46
    • 0033384878 scopus 로고    scopus 로고
    • A and 310: The split personality of polypeptide helices
    • Bolin, K. A. and Millhauser, G. L. (1999). a and 310: The split personality of polypeptide helices. Acc. Chem. Res. 32, 1027-33.
    • (1999) Acc. Chem. Res. , vol.32 , pp. 1027-1033
    • Bolin, K.A.1    Millhauser, G.L.2
  • 47
    • 0026783919 scopus 로고
    • Short alanine-based peptides may form 310-helices and not a-helices in aqueous solution
    • Miick, S. M., Martinez, G. V., Fiori, W. R., Todd, A. P., and Millhauser, G. L. (1992). Short alanine-based peptides may form 310-helices and not a-helices in aqueous solution. Nature 359, 653-5.
    • (1992) Nature , vol.359 , pp. 653-655
    • Miick, S.M.1    Martinez, G.V.2    Fiori, W.R.3    Todd, A.P.4    Millhauser, G.L.5
  • 48
  • 49
    • 0029439816 scopus 로고
    • Exploring the peptide 310-helix/a-helix equilibrium with double label electron spin resonance
    • Fiori, W. R. and Millhauser, G. L. (1995). Exploring the peptide 310-helix/a-helix equilibrium with double label electron spin resonance. Biopolymers 37, 243-50.
    • (1995) Biopolymers , vol.37 , pp. 243-250
    • Fiori, W.R.1    Millhauser, G.L.2
  • 52
    • 0001570011 scopus 로고
    • Generalized mathematical relations for polypeptide chain helixes. The coordinates for the p helix
    • Low, B. W. and Grenville-Wells, H. J. (1953). Generalized mathematical relations for polypeptide chain helixes. The coordinates for the p helix. Proc. Natl Acad. Sci. USA 39, 785-801.
    • (1953) Proc. Natl Acad. Sci. USA , vol.39 , pp. 785-801
    • Low, B.W.1    Grenville-Wells, H.J.2
  • 53
    • 0030970740 scopus 로고    scopus 로고
    • Curious structure in ''canonical'' alanine based peptides
    • Shirley, W. A. and Brooks, C. L. (1997). Curious structure in ''canonical'' alanine based peptides. Proteins: Struct. Funct. Genet. 28, 59-71.
    • (1997) Proteins: Struct. Funct. Genet. , vol.28 , pp. 59-71
    • Shirley, W.A.1    Brooks, C.L.2
  • 54
    • 0034649410 scopus 로고    scopus 로고
    • Transitions from a to p helix observed in molecular dynamics simulations of synthetic peptides
    • Lee, K. H., Benson, D. R., and Kuczera, K. (2000). Transitions from a to p helix observed in molecular dynamics simulations of synthetic peptides. Biochemistry 39, 13737-47.
    • (2000) Biochemistry , vol.39 , pp. 13737-13747
    • Lee, K.H.1    Benson, D.R.2    Kuczera, K.3
  • 55
    • 0033978466 scopus 로고    scopus 로고
    • The p-helix translates structure into function
    • Weaver, T. M. (2000). The p-helix translates structure into function. Protein Sci. 9, 201-6.
    • (2000) Protein Sci. , vol.9 , pp. 201-206
    • Weaver, T.M.1
  • 56
    • 0035923235 scopus 로고    scopus 로고
    • A designed Zn2{thorn}-binding amphiphilic polypeptide: Energetic consequences of p-helicity
    • Morgan, D. M., Lynn, D. G., Miller-Auer, H., and Meredith, S. C. (2001). A designed Zn2{thorn}-binding amphiphilic polypeptide: Energetic consequences of p-helicity. Biochemistry 40, 14020-9.
    • (2001) Biochemistry , vol.40 , pp. 14020-14029
    • Morgan, D.M.1    Lynn, D.G.2    Miller-Auer, H.3    Meredith, S.C.4
  • 57
    • 0036276409 scopus 로고    scopus 로고
    • Occurrence, conformational features and amino acid propensities for the p-helix
    • Fodje, M. N. and Al-Karadaghi, S. (2002). Occurrence, conformational features and amino acid propensities for the p-helix. Protein Eng. 15, 353-8.
    • (2002) Protein Eng. , vol.15 , pp. 353-358
    • Fodje, M.N.1    Al-Karadaghi, S.2
  • 58
    • 0037705435 scopus 로고    scopus 로고
    • In search of the energetic role of peptide hydrogen bonds
    • Baldwin, R. L. (2003). In search of the energetic role of peptide hydrogen bonds. J. Biol. Chem. 278, 17581-8.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17581-17588
    • Baldwin, R.L.1
  • 59
    • 0014317618 scopus 로고
    • Biochemistry
    • Epand, R. M. and Scheraga, H. A. (1968). Biochemistry 7, 2864-72.
    • (1968) , vol.7 , pp. 2864-2872
    • Epand, R.M.1    Scheraga, H.A.2
  • 61
    • 0013051990 scopus 로고
    • Intermolecular interactions in a helical oligo-and poly(L-glutamic acid) at acidic pH
    • Spek, E. J., Gong, Y., and Kallenbach, N. R. (1995). Intermolecular interactions in a helical oligo-and poly(L-glutamic acid) at acidic pH. J. Am. Chem. Soc. 117, 10773-4.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10773-10774
    • Spek, E.J.1    Gong, Y.2    Kallenbach, N.R.3
  • 62
    • 0015207557 scopus 로고
    • Biochemistry
    • Brown, J. E. and Klee, W. A. (1971). Biochemistry 10, 470-6.
    • (1971) , vol.10 , pp. 470-476
    • Brown, J.E.1    Klee, W.A.2
  • 63
    • 0020119906 scopus 로고
    • A salt bridge stabilizes the helix formed by isolated C-peptide of ribonuclease A
    • Bierzynski, A., Kim, P. S., and Baldwin, R. L. (1982). A salt bridge stabilizes the helix formed by isolated C-peptide of ribonuclease A. Proc. Natl Acad. Sci. USA 79, 2470-4.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 2470-2474
    • Bierzynski, A.1    Kim, P.S.2    Baldwin, R.L.3
  • 64
    • 0020410380 scopus 로고
    • A competing salt-bridge suppresses helix formation by the isolated C-peptide carboxylate of Ribonuclease A
    • Kim, P. S., Bierzynski, A., and Baldwin, R. L. (1982). A competing salt-bridge suppresses helix formation by the isolated C-peptide carboxylate of Ribonuclease A. J. Mol. Biol. 162, 187-99.
    • (1982) J. Mol. Biol. , vol.162 , pp. 187-199
    • Kim, P.S.1    Bierzynski, A.2    Baldwin, R.L.3
  • 65
    • 0021281005 scopus 로고
    • A helix stop signal in the isolated Speptide of ribonuclease A
    • Kim, P. S. and Baldwin, R. L. (1984). A helix stop signal in the isolated Speptide of ribonuclease A. Nature 307, 329-34.
    • (1984) Nature , vol.307 , pp. 329-334
    • Kim, P.S.1    Baldwin, R.L.2
  • 66
    • 0000640899 scopus 로고
    • Nature of the charged-group effect on the stability of the C-peptide helix
    • Shoemaker, K. R., Kim, P. S., Brems, D. N. et al. (1985). Nature of the charged-group effect on the stability of the C-peptide helix. Proc. Natl Acad. Sci. USA 82, 2349-53.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 2349-2353
    • Shoemaker, K.R.1    Kim, P.S.2    Brems, D.N.3
  • 67
    • 0024553005 scopus 로고
    • Effect of the substitution Ala-Gly at each of 5 residue positions in the C-peptide helix
    • Strehlow, K. G. and Baldwin, R. L. (1989). Effect of the substitution Ala-Gly at each of 5 residue positions in the C-peptide helix. Biochemistry 28, 2130-3.
    • (1989) Biochemistry , vol.28 , pp. 2130-2133
    • Strehlow, K.G.1    Baldwin, R.L.2
  • 68
    • 0024472052 scopus 로고
    • H-1 NMR studies of the solution conformations of an analog of the C-peptide of ribonuclease-A
    • Osterhout, J. J., Baldwin, R. L., York, E. J., Stewart, J. M., Dyson, H. J., and Wright, P. E. (1989). H-1 NMR studies of the solution conformations of an analog of the C-peptide of ribonuclease-A. Biochemistry 29, 7059-64.
    • (1989) Biochemistry , vol.29 , pp. 7059-7064
    • Osterhout, J.J.1    Baldwin, R.L.2    York, E.J.3    Stewart, J.M.4    Dyson, H.J.5    Wright, P.E.6
  • 69
    • 0025181558 scopus 로고
    • Sidechain interactions in the C-peptide helix-Phe8-His12{thorn}
    • Shoemaker, K. R., Fairman, R., Schultz, D. A. et al. (1990). Sidechain interactions in the C-peptide helix-Phe8-His12{thorn}. Biopolymers 29, 1-11.
    • (1990) Biopolymers , vol.29 , pp. 1-11
    • Shoemaker, K.R.1    Fairman, R.2    Schultz, D.A.3
  • 70
    • 0025196527 scopus 로고
    • The Glu2-Arg10{thorn} side-chain interaction in the C-peptide helix of ribonuclease A
    • Fairman, R., Shoemaker, K. R., York, E. J., Stewart, J. M., and Baldwin, R. L. (1990). The Glu2-Arg10{thorn} side-chain interaction in the C-peptide helix of ribonuclease A. Biophys. Chem. 37, 107-19.
    • (1990) Biophys. Chem. , vol.37 , pp. 107-119
    • Fairman, R.1    Shoemaker, K.R.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 71
    • 0025808091 scopus 로고
    • Proline for alanine subsitutions in the C-peptide helix of ribonuclease A
    • Strehlow, K. G., Robertson, A. D., and Baldwin, R. L. (1991). Proline for alanine subsitutions in the C-peptide helix of ribonuclease A. Biochemistry 30, 5810-14.
    • (1991) Biochemistry , vol.30 , pp. 5810-5814
    • Strehlow, K.G.1    Robertson, A.D.2    Baldwin, R.L.3
  • 73
    • 0026521337 scopus 로고
    • The homologous angiogenin and ribonuclease Nterminal fragments fold into very similar helices when isolated
    • Blanco, F. J., Jimenez, M. A., Rico, M., Santoro, J., Herranz, J., and Nieto, J. L. (1992). The homologous angiogenin and ribonuclease Nterminal fragments fold into very similar helices when isolated. Biochem. Biophys. Res. Commun. 182, 1491-8.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1491-1498
    • Blanco, F.J.1    Jimenez, M.A.2    Rico, M.3    Santoro, J.4    Herranz, J.5    Nieto, J.L.6
  • 74
    • 84986786292 scopus 로고
    • H1-NMR parameters of the N-terminal 13-residue C-peptide of ribonuclease in aqueous-solution
    • Rico, M., Nieto, J. L., Santoro, J., Bermejo, F. J., and Herranz, J. (1983). H1-NMR parameters of the N-terminal 13-residue C-peptide of ribonuclease in aqueous-solution. Org. Magn. Res. 21, 555-63.
    • (1983) Org. Magn. Res. , vol.21 , pp. 555-563
    • Rico, M.1    Nieto, J.L.2    Santoro, J.3    Bermejo, F.J.4    Herranz, J.5
  • 75
    • 0020728140 scopus 로고
    • H1-NMR parameters of the N-terminal 19-residue S-peptide of ribonuclease in aqueous-solution
    • Gallego, E., Herranz, J., Nieto, J. L., Rico, M., and Santoro, J. (1983). H1-NMR parameters of the N-terminal 19-residue S-peptide of ribonuclease in aqueous-solution. Int. J. Pept. Protein Res. 21, 242-53.
    • (1983) Int. J. Pept. Protein Res. , vol.21 , pp. 242-253
    • Gallego, E.1    Herranz, J.2    Nieto, J.L.3    Rico, M.4    Santoro, J.5
  • 76
    • 0021106990 scopus 로고
    • Low temperature H1-NMR evidence of the folding of isolated ribonuclease S-peptide
    • Rico, M., Nieto, J. L., Santoro, J., Bermejo, F. J., Herranz, J., and Gallego, E. (1983). Low temperature H1-NMR evidence of the folding of isolated ribonuclease S-peptide. FEBS Lett. 162, 314-19.
    • (1983) FEBS Lett. , vol.162 , pp. 314-319
    • Rico, M.1    Nieto, J.L.2    Santoro, J.3    Bermejo, F.J.4    Herranz, J.5    Gallego, E.6
  • 77
    • 0021765972 scopus 로고
    • On the fundamental role of the Glu2-.. Arg10{thorn} salt bridge in the folding of isolated ribonuclease A S-peptide
    • Rico, M., Gallego, E., Santoro, J., Bermejo, F. J., Nieto, J. L., and Herranz, J. (1984). On the fundamental role of the Glu2-... Arg10{thorn} salt bridge in the folding of isolated ribonuclease A S-peptide. Biochem. Biophys. Res. Commun. 123, 757-63.
    • (1984) Biochem. Biophys. Res. Commun. , vol.123 , pp. 757-763
    • Rico, M.1    Gallego, E.2    Santoro, J.3    Bermejo, F.J.4    Nieto, J.L.5    Herranz, J.6
  • 79
    • 0021979995 scopus 로고
    • NH resonanaces of ribonuclease S-peptide in aqueous solution-low temperature NMR study
    • Nieto, J. L., Rico, M., Santoro, J., and Bermejo, J. (1985). NH resonanaces of ribonuclease S-peptide in aqueous solution-low temperature NMR study. Int. J. Pept. Protein Res. 25, 47-55.
    • (1985) Int. J. Pept. Protein Res. , vol.25 , pp. 47-55
    • Nieto, J.L.1    Rico, M.2    Santoro, J.3    Bermejo, J.4
  • 80
    • 46149134863 scopus 로고
    • C13 NMR spectral assignment of ribonuclease S-peptide-Some new structural information about its low temperature folding
    • Santoro, J., Rico, M., Nieto, J. L., Bermejo, J., Herranz, J., and Gallego, E. (1986). C13 NMR spectral assignment of ribonuclease S-peptide-Some new structural information about its low temperature folding. J. Mol. Struct. 141, 243-8.
    • (1986) J. Mol. Struct. , vol.141 , pp. 243-248
    • Santoro, J.1    Rico, M.2    Nieto, J.L.3    Bermejo, J.4    Herranz, J.5    Gallego, E.6
  • 81
    • 46149139248 scopus 로고
    • Quantitative interpretation of the helix coil transition in RNase A S-peptide
    • Rico, M., Herranz, J., Bermejo, J. et al. (1986). Quantitative interpretation of the helix coil transition in RNase A S-peptide. J. Mol. Struct. 143, 439-44.
    • (1986) J. Mol. Struct. , vol.143 , pp. 439-444
    • Rico, M.1    Herranz, J.2    Bermejo, J.3
  • 82
    • 0022728643 scopus 로고
    • Thermodynamic parameters for the helix coil thermal transition of ribonuclease S-peptide and derivatives from H1 NMR data
    • Rico, M., Santoro, J., Bermejo, J. et al. (1986). Thermodynamic parameters for the helix coil thermal transition of ribonuclease S-peptide and derivatives from H1 NMR data. Biopolymers 25, 1031-53.
    • (1986) Biopolymers , vol.25 , pp. 1031-1053
    • Rico, M.1    Santoro, J.2    Bermejo, J.3
  • 83
    • 0023461350 scopus 로고
    • Helix stabilization by Glu-.. Lys{thorn} salt bridges in short peptides of de novo design
    • Marqusee, S. and Baldwin, R. L. (1987). Helix stabilization by Glu-... Lys{thorn} salt bridges in short peptides of de novo design. Proc. Natl Acad. Sci. USA 84, 8898-902.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 8898-8902
    • Marqusee, S.1    Baldwin, R.L.2
  • 84
    • 0027249564 scopus 로고
    • Residue helix parameters obtained from dichroic analysis of peptides of defined sequence
    • Park, S. H., Shalongo, W., and Stellwagen, E. (1993). Residue helix parameters obtained from dichroic analysis of peptides of defined sequence. Biochemistry 32, 7048-53.
    • (1993) Biochemistry , vol.32 , pp. 7048-7053
    • Park, S.H.1    Shalongo, W.2    Stellwagen, E.3
  • 85
    • 0024707204 scopus 로고
    • Unusually stable helix formation in short alanine based peptides
    • Marqusee, S., Robbins, V. H., and Baldwin, R. L. (1989). Unusually stable helix formation in short alanine based peptides. Proc. Natl Acad. Sci. USA 86, 5286-90.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 5286-5290
    • Marqusee, S.1    Robbins, V.H.2    Baldwin, R.L.3
  • 86
    • 0000599471 scopus 로고
    • The role of ion-pairs in a-helix stability-2 new designed helical peptides
    • Lyu, P. C., Marky, L. A., and Kallen-bach, N. R. (1989). The role of ion-pairs in a-helix stability-2 new designed helical peptides. J. Am. Chem. Soc. 111, 2733-34.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 2733-2734
    • Lyu, P.C.1    Marky, L.A.2    Kallen-bach, N.R.3
  • 87
    • 0025260032 scopus 로고
    • Sidechain contributions to the stability of a-helical structure in peptides
    • Lyu, P. C., Liff, M. I., Marky, L. A., and Kallenbach, N. R. (1990). Sidechain contributions to the stability of a-helical structure in peptides. Science 250, 669-73.
    • (1990) Science , vol.250 , pp. 669-673
    • Lyu, P.C.1    Liff, M.I.2    Marky, L.A.3    Kallenbach, N.R.4
  • 88
    • 0026253633 scopus 로고
    • The helix-coil transition in heterogeneous peptides with specific side chain interactions: Theory and comparison with circular dichroism
    • Gans, P. J., Lyu, P. C., Manning, P. C., Woody, R. W., and Kallenbach, N. R. (1991). The helix-coil transition in heterogeneous peptides with specific side chain interactions: Theory and comparison with circular dichroism. Biopolymers 31, 1605-14.
    • (1991) Biopolymers , vol.31 , pp. 1605-1614
    • Gans, P.J.1    Lyu, P.C.2    Manning, P.C.3    Woody, R.W.4    Kallenbach, N.R.5
  • 90
    • 0017292056 scopus 로고
    • The a-helix as an electric macro-dipole
    • Wada, A. (1976). The a-helix as an electric macro-dipole. Adv. Biophys. 9, 1-63.
    • (1976) Adv. Biophys. , vol.9 , pp. 1-63
    • Wada, A.1
  • 91
    • 0017881332 scopus 로고
    • The a-helix dipole and the properties of proteins
    • Hol, W. G. J., van Duijnen, P. T., and Berendsen, H. J. C. (1978). The a-helix dipole and the properties of proteins. Nature 273, 443-6.
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.J.1    Van Duijnen, P.T.2    Berendsen, H.J.C.3
  • 92
  • 93
    • 0027980822 scopus 로고
    • Contribution to global protein stabilization of the N-capping box in human growth hormone
    • Zhukovsky, E. A., Mulkerrin, M. G., and Presta, L. G. (1994). Contribution to global protein stabilization of the N-capping box in human growth hormone. Biochemistry 33, 9856-64.
    • (1994) Biochemistry , vol.33 , pp. 9856-9864
    • Zhukovsky, E.A.1    Mulkerrin, M.G.2    Presta, L.G.3
  • 94
    • 0028027354 scopus 로고
    • Helix-capping interaction in l Cro protein: a free energy simulation analysis
    • Tidor, B. (1994). Helix-capping interaction in l Cro protein: a free energy simulation analysis. Proteins: Struct. Funct. Genet. 19, 310-23.
    • (1994) Proteins: Struct. Funct. Genet. , vol.19 , pp. 310-323
    • Tidor, B.1
  • 95
    • 0035106699 scopus 로고    scopus 로고
    • Contribution of the N1 amino acid residue to the stability of the a-helix
    • Cochran, D. A. E., Penel, S., and Doig, A. J. (2001). Contribution of the N1 amino acid residue to the stability of the a-helix. Protein Sci. 10, 463-70.
    • (2001) Protein Sci. , vol.10 , pp. 463-470
    • Cochran, D.A.E.1    Penel, S.2    Doig, A.J.3
  • 96
    • 0034974668 scopus 로고    scopus 로고
    • Effects of the N2 residue on the stability of the a-helix for all 20 amino acids
    • Cochran, D. A. E. and Doig, A. J. (2001). Effects of the N2 residue on the stability of the a-helix for all 20 amino acids. Protein Sci. 10, 1305-11.
    • (2001) Protein Sci. , vol.10 , pp. 1305-1311
    • Cochran, D.A.E.1    Doig, A.J.2
  • 97
    • 0346733335 scopus 로고    scopus 로고
    • Effect of the N3 residue on the stability of the a-helix
    • (in press)
    • Iqbalsyah, T. M. and Doig, A. J. (in press). Effect of the N3 residue on the stability of the a-helix. Protein Sci. 13, 32-39.
    • Protein Sci. , vol.13 , pp. 32-39
    • Iqbalsyah, T.M.1    Doig, A.J.2
  • 98
    • 0034285165 scopus 로고    scopus 로고
    • IR spectroscopy of isotope-labeled helical peptides: Probing the effect of Nacetylation on helix stability
    • Biopolymers
    • Decatur, S. M. (2000). IR spectroscopy of isotope-labeled helical peptides: Probing the effect of Nacetylation on helix stability. Biopolymers 180-5.
    • (2000) , pp. 180-185
    • Decatur, S.M.1
  • 99
    • 0028289435 scopus 로고
    • Determination of free energies of N-capping in a-helices by modification of the Lifson-Roig helix-coil theory to include N-and C-capping
    • Doig, A. J., Chakrabartty, A., Klingler, T. M., and Baldwin, R. L. (1994). Determination of free energies of N-capping in a-helices by modification of the Lifson-Roig helix-coil theory to include N-and C-capping. Biochemistry 33, 3396-403.
    • (1994) Biochemistry , vol.33 , pp. 3396-3403
    • Doig, A.J.1    Chakrabartty, A.2    Klingler, T.M.3    Baldwin, R.L.4
  • 100
    • 0028822255 scopus 로고
    • Addition of side chain interactions to modified Lifson-Roig helix-coil theory: application to energetics of phenylalanine-methionine interactions
    • Stapley, B. J., Rohl, C. A., and Doig, A. J. (1995). Addition of side chain interactions to modified Lifson-Roig helix-coil theory: application to energetics of phenylalanine-methionine interactions. Protein Sci. 4, 2383-91.
    • (1995) Protein Sci. , vol.4 , pp. 2383-2391
    • Stapley, B.J.1    Rohl, C.A.2    Doig, A.J.3
  • 102
    • 0027359429 scopus 로고
    • Effect of a single aspartate on helix stability at different positions in a neutral alanine-based peptide
    • Huyghues-Despointes, B. M., Scholtz, J. M., and Baldwin, R. L. (1993). Effect of a single aspartate on helix stability at different positions in a neutral alanine-based peptide. Protein Sci. 2, 1604-11.
    • (1993) Protein Sci. , vol.2 , pp. 1604-1611
    • Huyghues-Despointes, B.M.1    Scholtz, J.M.2    Baldwin, R.L.3
  • 103
    • 0001046251 scopus 로고
    • Derivative spectroscopy applied to tyrosyl chromophores. Studies on ribonuclease, lima bean inhibitor, and pancreatic trypsin inhibitor
    • Brandts, J. R. and Kaplan, K. J. (1973). Derivative spectroscopy applied to tyrosyl chromophores. Studies on ribonuclease, lima bean inhibitor, and pancreatic trypsin inhibitor. Biochemistry 10, 470-6.
    • (1973) Biochemistry , vol.10 , pp. 470-476
    • Brandts, J.R.1    Kaplan, K.J.2
  • 104
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967). Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6, 1948-54.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 105
    • 0027298784 scopus 로고
    • Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities
    • Chakrabartty, A., Kortemme, T., Padmanabhan, S., and Baldwin, R. L. (1993). Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities. Biochemistry 32, 5560-5.
    • (1993) Biochemistry , vol.32 , pp. 5560-5565
    • Chakrabartty, A.1    Kortemme, T.2    Padmanabhan, S.3    Baldwin, R.L.4
  • 106
    • 0037202199 scopus 로고    scopus 로고
    • Stabilising interactions between aromatic and basic side chains in a-helical peptides and proteins. Tyrosine effects on helix circular dichroism
    • Andrew, C. D., Bhattacharjee, S., Kokkoni, N., Hirst, J. D., Jones, G. R., and Doig, A. J. (2002). Stabilising interactions between aromatic and basic side chains in a-helical peptides and proteins. Tyrosine effects on helix circular dichroism. J. Am. Chem. Soc. 124, 12706-14.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12706-12714
    • Andrew, C.D.1    Bhattacharjee, S.2    Kokkoni, N.3    Hirst, J.D.4    Jones, G.R.5    Doig, A.J.6
  • 107
    • 0026209013 scopus 로고
    • The helical s-constant for alanine in water derived from template-nucleated helices
    • Kemp, D. S., Boyd, J. G., and Muendel, C. C. (1991). The helical s-constant for alanine in water derived from template-nucleated helices. Nature 352, 451-4.
    • (1991) Nature , vol.352 , pp. 451-454
    • Kemp, D.S.1    Boyd, J.G.2    Muendel, C.C.3
  • 108
    • 0028850960 scopus 로고
    • The energetics of helix formation by short templated peptides in aqueous solution. 1. Characterization of the reporting helical template Ac-HE1(1)
    • Kemp, D. S., Allen, T. J., and Oslick, S. L. (1995). The energetics of helix formation by short templated peptides in aqueous solution. 1. Characterization of the reporting helical template Ac-HE1(1). J. Am. Chem. Soc. 117, 6641-57.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6641-6657
    • Kemp, D.S.1    Allen, T.J.2    Oslick, S.L.3
  • 109
    • 0029863726 scopus 로고    scopus 로고
    • Templatenucleated alanine-lysine helices are stabilized by position-dependent interactions between the lysine side chain and the helix barrel
    • Groebke, K., Renold, P., Tsang, K. Y., Allen, T. J., McClure, K. F., and Kemp, D. S. (1996). Templatenucleated alanine-lysine helices are stabilized by position-dependent interactions between the lysine side chain and the helix barrel. Proc. Natl Acad. Sci. USA 93, 4025-9.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4025-4029
    • Groebke, K.1    Renold, P.2    Tsang, K.Y.3    Allen, T.J.4    McClure, K.F.5    Kemp, D.S.6
  • 110
    • 0029949745 scopus 로고    scopus 로고
    • 3. Calculation of the helical propagation constant s from the template stability constants t/c for Ac-Hel(1)-Ala(n)-OH, n 1/4 1-6
    • Kemp, D. S., Oslick, S. L., and Allen, T. J. (1996). The structure and energetics of helix formation by short templated peptides in aqueous soluti. 3. Calculation of the helical propagation constant s from the template stability constants t/c for Ac-Hel(1)-Ala(n)-OH, n 1/4 1-6. J. Am. Chem. Soc. 118, 4249-55.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 4249-4255
    • Kemp, D.S.1    Oslick, S.L.2    Allen, T.J.3
  • 111
    • 15844412825 scopus 로고    scopus 로고
    • The structure and energetics of helix formation by short templated peptides in aqueous solution. 2. Characterization of the helical structure of Ac-Hel(1)-Ala(6)-OH
    • Kemp, D. S., Allen, T. J., Oslick, S. L., and Boyd, J. G. (1996). The structure and energetics of helix formation by short templated peptides in aqueous solution. 2. Characterization of the helical structure of Ac-Hel(1)-Ala(6)-OH. J. Am. Chem. Soc. 118, 4240-8.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 4240-4248
    • Kemp, D.S.1    Allen, T.J.2    Oslick, S.L.3    Boyd, J.G.4
  • 112
    • 0030879441 scopus 로고    scopus 로고
    • Template for stabilization of a peptide a-helix: Synthesis and evaluation of conformational effects by circular dichroism and NMR
    • Austin, R. E., Maplestone, R. A., Sefler, A. M. et al. (1997). Template for stabilization of a peptide a-helix: Synthesis and evaluation of conformational effects by circular dichroism and NMR. J. Am. Chem. Soc. 119, 6461-72.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6461-6472
    • Austin, R.E.1    Maplestone, R.A.2    Sefler, A.M.3
  • 113
    • 84889797250 scopus 로고
    • Peptides: Chemistry, Structure and Biolog y: Proceedings of the 11th American Peptide Symposium
    • ESCOM, Leiden
    • Arrhenius, T. and Sattherthwait, A. C. (1990). Peptides: Chemistry, Structure and Biolog y: Proceedings of the 11th American Peptide Symposium, ESCOM, Leiden.
    • (1990)
    • Arrhenius, T.1    Sattherthwait, A.C.2
  • 114
    • 0003653371 scopus 로고
    • Perspectives in Medicinal Chemistry
    • Verlag Chemie, Weinheim
    • Muller, K., Obrecht, D., Knierzinger, A. et al. (1993). Perspectives in Medicinal Chemistry, pp. 513-531, Verlag Chemie, Weinheim.
    • (1993) , pp. 513-531
    • Muller, K.1    Obrecht, D.2    Knierzinger, A.3
  • 115
    • 0032564579 scopus 로고    scopus 로고
    • Design, synthesis, structure and properties of an a-helix cap template derived from N-[(2S)-2-chloropropionyl]-(2S)-Pro-(2R)-Ala-(2S,4S)-4-thioPro-OMe which initiates a-helical structures
    • Gani, D., Lewis, A., Rutherford, T. et al. (1998). Design, synthesis, structure and properties of an a-helix cap template derived from N-[(2S)-2-chloropropionyl]-(2S)-Pro-(2R)-Ala-(2S,4S)-4-thioPro-OMe which initiates a-helical structures. Tetrahedron 54, 15793-819.
    • (1998) Tetrahedron , vol.54 , pp. 15793-15819
    • Gani, D.1    Lewis, A.2    Rutherford, T.3
  • 116
    • 0001722942 scopus 로고    scopus 로고
    • Conformational properties of a-amino acids disubstituted at the a-carbon
    • Aleman, C. (1997). Conformational properties of a-amino acids disubstituted at the a-carbon. J. Phys. Chem. 101, 5046-50.
    • (1997) J. Phys. Chem. , vol.101 , pp. 5046-5050
    • Aleman, C.1
  • 117
    • 0001274619 scopus 로고    scopus 로고
    • Linear oligopeptide. 401. In search of a peptide 310-helix in water
    • Sacca, B., Formaggio, F., Crisma, M., Toniolo, C., and Gennaro, R. (1997). Linear oligopeptide. 401. In search of a peptide 310-helix in water. Gazz. Chim. Ital. 127, 495-500.
    • (1997) Gazz. Chim. Ital. , vol.127 , pp. 495-500
    • Sacca, B.1    Formaggio, F.2    Crisma, M.3    Toniolo, C.4    Gennaro, R.5
  • 118
    • 0036486718 scopus 로고    scopus 로고
    • Design and conformation of peptides containing a, a-disubstituted a-amino acids
    • Tanaka, M. (2002). Design and conformation of peptides containing a, a-disubstituted a-amino acids. J. Synth. Org. Chem. Japan 60, 125-36.
    • (2002) J. Synth. Org. Chem. Japan , vol.60 , pp. 125-136
    • Tanaka, M.1
  • 119
    • 0038050381 scopus 로고    scopus 로고
    • Characterization of the 310-helix in model peptides by HRMAS NMR spectroscopy
    • Lancelot, N., Elbayed, K., Raya, J. et al. (2003). Characterization of the 310-helix in model peptides by HRMAS NMR spectroscopy. Chem. Eur. J. 9, 1317-23.
    • (2003) Chem. Eur. J. , vol.9 , pp. 1317-1323
    • Lancelot, N.1    Elbayed, K.2    Raya, J.3
  • 120
    • 0025345233 scopus 로고
    • Structural characteristics of a-helical peptide molecules containing Aib residues
    • Karle, I. L. and Balaram, P. (1990). Structural characteristics of a-helical peptide molecules containing Aib residues. Biochemistry 29, 6747-56.
    • (1990) Biochemistry , vol.29 , pp. 6747-6756
    • Karle, I.L.1    Balaram, P.2
  • 121
    • 0037011545 scopus 로고    scopus 로고
    • A short Aib/Ala-based peptide helix is as stable as an Ala-based peptide helix double its length
    • Banerjee, R. and Basu, G. (2002). A short Aib/Ala-based peptide helix is as stable as an Ala-based peptide helix double its length. ChemBiochem 3, 1263-6.
    • (2002) ChemBiochem , vol.3 , pp. 1263-1266
    • Banerjee, R.1    Basu, G.2
  • 122
    • 0031018028 scopus 로고    scopus 로고
    • Solvent effects on the 310-/a-helix equilibrium in short amphipathic peptides rich in a, adisubstituted amino acids
    • Yokum, T. S., Gauthier, T. J., Hammer, R. P., and McLaughlin, M. L. (1997). Solvent effects on the 310-/a-helix equilibrium in short amphipathic peptides rich in a, adisubstituted amino acids. J. Am. Chem. Soc. 119, 1167-8.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 1167-1168
    • Yokum, T.S.1    Gauthier, T.J.2    Hammer, R.P.3    McLaughlin, M.L.4
  • 123
    • 0031564662 scopus 로고    scopus 로고
    • Estimating the relative populations of 310-helix and ahelix in Ala-rich peptides. A hydrogen exchange and high field NMR study
    • Millhauser, G. L., Stenland, C. J., Hanson, P., Bolin, K. A., and van de Ven, F. J. M. (1997). Estimating the relative populations of 310-helix and ahelix in Ala-rich peptides. A hydrogen exchange and high field NMR study. J. Mol. Biol. 267, 963-74.
    • (1997) J. Mol. Biol. , vol.267 , pp. 963-974
    • Millhauser, G.L.1    Stenland, C.J.2    Hanson, P.3    Bolin, K.A.4    van de Ven, F.J.M.5
  • 124
    • 0028447414 scopus 로고
    • A single carboxy-terminal arginine determines the amino-terminal helix conformation of an alanine-based peptide
    • Fiori, W. R., Lundberg, K. M., and Millhauser, G. L. (1994). A single carboxy-terminal arginine determines the amino-terminal helix conformation of an alanine-based peptide. Nat. Struct. Biol. 1, 374-7.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 374-377
    • Fiori, W.R.1    Lundberg, K.M.2    Millhauser, G.L.3
  • 125
    • 0030668705 scopus 로고    scopus 로고
    • Conformation characterization of terminally blocked L-(aMe)Val homopeptides using vibrational and electronic circular dichroism. 310-Helical stabilization by peptide-peptide interaction.
    • Yoder, G., Polese, A., Silva, R. A. G. D. et al. (1997). Conformation characterization of terminally blocked L-(aMe)Val homopeptides using vibrational and electronic circular dichroism. 310-Helical stabilization by peptide-peptide interaction. J. Am. Chem. Soc. 119, 10278-85.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 10278-10285
    • Yoder, G.1    Polese, A.2    Silva, R.A.G.D.3
  • 126
    • 0025880710 scopus 로고
    • Studies of peptides forming 310-and a-helices and b-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy
    • Kennedy, D. F., Crisma, M., Toniolo, C., and Chapman, D. (1991). Studies of peptides forming 310-and a-helices and b-bend ribbon structures in organic solution and in model biomembranes by Fourier transform infrared spectroscopy. Biochemistry 30, 6541-8.
    • (1991) Biochemistry , vol.30 , pp. 6541-6548
    • Kennedy, D.F.1    Crisma, M.2    Toniolo, C.3    Chapman, D.4
  • 127
    • 33751147994 scopus 로고    scopus 로고
    • A reversible transition between an a-helix and a 310-helix in a fluorescence-labelled peptide
    • Hungerford, G., Martinez-Insua, M., Birch, D. J. S., and Moore, B. D. (1996). A reversible transition between an a-helix and a 310-helix in a fluorescence-labelled peptide. Angew. Chem. Int. Ed. Engl. 35, 326-9.
    • (1996) Angew. Chem. Int. Ed. Engl. , vol.35 , pp. 326-329
    • Hungerford, G.1    Martinez-Insua, M.2    Birch, D.J.S.3    Moore, B.D.4
  • 128
    • 0028814090 scopus 로고
    • 310-Helices in peptides and proteins as studied by modified Zimm-Bragg theory
    • Sheinerman, F. B. and Brooks, C. L. (1995). 310-Helices in peptides and proteins as studied by modified Zimm-Bragg theory. J. Am. Chem. Soc. 117, 10098-103.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10098-10103
    • Sheinerman, F.B.1    Brooks, C.L.2
  • 130
  • 131
    • 0031181666 scopus 로고    scopus 로고
    • Protein folding and the paracelsus challenge
    • Rose, G. D. (1997). Protein folding and the paracelsus challenge. Nat. Struct. Biol. 4, 512-14.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 512-514
    • Rose, G.D.1
  • 132
    • 0003517850 scopus 로고
    • Theory of Helix-Coil Transitions in Biopolymers
    • Academic Press, New York and London
    • Poland, D. and Scheraga, H. A. (1970). Theory of Helix-Coil Transitions in Biopolymers. Academic Press, New York and London.
    • (1970)
    • Poland, D.1    Scheraga, H.A.2
  • 133
    • 33751391161 scopus 로고
    • Helix/coil theories: A comparative study for finite length polypeptides
    • Qian, H. and Schellman, J. A. (1992). Helix/coil theories: A comparative study for finite length polypeptides. J. Phys. Chem. 96, 3987-94.
    • (1992) J. Phys. Chem. , vol.96 , pp. 3987-3994
    • Qian, H.1    Schellman, J.A.2
  • 134
    • 0037059026 scopus 로고    scopus 로고
    • Recent advances in helix-coil theory
    • Doig, A. J. (2002). Recent advances in helix-coil theory. Biophys. Chem. 101-102, 281-93.
    • (2002) Biophys. Chem. , vol.101-102 , pp. 281-293
    • Doig, A.J.1
  • 135
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm, B. H. and Bragg, J. K. (1959). Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31, 526-35.
    • (1959) J. Chem. Phys. , vol.31 , pp. 526-535
    • Zimm, B.H.1    Bragg, J.K.2
  • 136
    • 0000333671 scopus 로고
    • On the theory of the helix-coil transition in polypeptides
    • Lifson, S. and Roig, A. (1961). On the theory of the helix-coil transition in polypeptides. J. Chem. Phys. 34, 1963-74.
    • (1961) J. Chem. Phys. , vol.34 , pp. 1963-1974
    • Lifson, S.1    Roig, A.2
  • 137
    • 0003478685 scopus 로고
    • Statistical Mechanics of Chain Molecules
    • Wiley, New York
    • Flory, P. J. (1969). Statistical Mechanics of Chain Molecules. Wiley, New York.
    • (1969)
    • Flory, P.J.1
  • 138
    • 0033730431 scopus 로고    scopus 로고
    • The Flory isolatedpair hypothesis is not valid for polypeptide chains: Implications for protein folding
    • Pappu, R. V., Srinivasan, R., and Rose, G. D. (2000). The Flory isolatedpair hypothesis is not valid for polypeptide chains: Implications for protein folding. Proc. Natl Acad. Sci. USA 97, 12565-70.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 12565-12570
    • Pappu, R.V.1    Srinivasan, R.2    Rose, G.D.3
  • 139
    • 0014227144 scopus 로고
    • New chain conformations of poly(glutamic acid) and polylysine
    • Tiffany, M. L. and Krimm, S. (1968). New chain conformations of poly(glutamic acid) and polylysine. Biopolymers 6, 1379-82.
    • (1968) Biopolymers , vol.6 , pp. 1379-1382
    • Tiffany, M.L.1    Krimm, S.2
  • 140
    • 84987322752 scopus 로고
    • The circular dichroism spectrum and structure of unordered polypeptides and proteins
    • Krimm, S. and Tiffany, M. L. (1974). The circular dichroism spectrum and structure of unordered polypeptides and proteins. Israel J. Chem. 12, 189-200.
    • (1974) Israel J. Chem. , vol.12 , pp. 189-200
    • Krimm, S.1    Tiffany, M.L.2
  • 141
    • 0002251831 scopus 로고
    • Circular dichroism and conformations of unordered polypeptides
    • Woody, R. W. (1992). Circular dichroism and conformations of unordered polypeptides. Adv. Biophys. Chem. 2, 37-79.
    • (1992) Adv. Biophys. Chem. , vol.2 , pp. 37-79
    • Woody, R.W.1
  • 142
    • 0034118337 scopus 로고    scopus 로고
    • Solution structure and dynamics of biomolecules from Raman optical activity
    • Barron, L. D., Hecht, L., Blanch, E. W., and Bell, A. F. (2000). Solution structure and dynamics of biomolecules from Raman optical activity. Prog. Biophys. Mol. Biol. 73, 1-49.
    • (2000) Prog. Biophys. Mol. Biol. , vol.73 , pp. 1-49
    • Barron, L.D.1    Hecht, L.2    Blanch, E.W.3    Bell, A.F.4
  • 143
    • 0034636977 scopus 로고    scopus 로고
    • Is polyproline II helix the killer conformation? A Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme
    • Blanch, E. W., Morozova-Roche, L. A., Cochran, D. A. E., Doig, A. J., Hecht, L., and Barron, L. D. (2000). Is polyproline II helix the killer conformation? A Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme. J. Mol. Biol. 301, 553-63.
    • (2000) J. Mol. Biol. , vol.301 , pp. 553-563
    • Blanch, E.W.1    Morozova-Roche, L.A.2    Cochran, D.A.E.3    Doig, A.J.4    Hecht, L.5    Barron, L.D.6
  • 144
    • 0035144719 scopus 로고    scopus 로고
    • Solution structure of native proteins irregular folds from Raman optical activity
    • Smyth, E., Syme, C. D., Blanch, E. W., Hecht, L., Vasak, M., and Barron, L. D. (2000). Solution structure of native proteins irregular folds from Raman optical activity. Biopolymers 58, 138-51.
    • (2000) Biopolymers , vol.58 , pp. 138-151
    • Smyth, E.1    Syme, C.D.2    Blanch, E.W.3    Hecht, L.4    Vasak, M.5    Barron, L.D.6
  • 145
    • 0036157963 scopus 로고    scopus 로고
    • A Raman optical activity study of the rheomorphism in caseins, synucleins and tau
    • Syme, C. D., Blanch, E. W., Holt, C. et al. (2002). A Raman optical activity study of the rheomorphism in caseins, synucleins and tau. Eur. J. Biochem. 269, 148-56.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 148-156
    • Syme, C.D.1    Blanch, E.W.2    Holt, C.3
  • 146
    • 0036129072 scopus 로고    scopus 로고
    • Polyproline II helical structure in protein unfolded states: Lysine peptides revisited
    • Rucker, A. L. and Creamer, T. P. (2002). Polyproline II helical structure in protein unfolded states: Lysine peptides revisited. Protein Sci. 11, 980-5.
    • (2002) Protein Sci. , vol.11 , pp. 980-985
    • Rucker, A.L.1    Creamer, T.P.2
  • 147
    • 0036400325 scopus 로고    scopus 로고
    • Is polyproline II a major backbone conformation in unfolded proteins?
    • Shi, Z. S., Woody, R. W., and Kallenbach, N. R. (2002). Is polyproline II a major backbone conformation in unfolded proteins? Adv. Protein Chem. 62, 163-240.
    • (2002) Adv. Protein Chem. , vol.62 , pp. 163-240
    • Shi, Z.S.1    Woody, R.W.2    Kallenbach, N.R.3
  • 148
    • 0036784642 scopus 로고    scopus 로고
    • A simple model for polyproline II structure in unfolded states of alaninebased peptides
    • Pappu, R. V. and Rose, G. D. (2002). A simple model for polyproline II structure in unfolded states of alaninebased peptides. Protein Sci. 11, 2437-55.
    • (2002) Protein Sci. , vol.11 , pp. 2437-2455
    • Pappu, R.V.1    Rose, G.D.2
  • 151
    • 0030767756 scopus 로고    scopus 로고
    • Empirical parameterization of a model for predicting peptide helix/coil equilibrium populations
    • Andersen, N. H. and Tong, H. (1997). Empirical parameterization of a model for predicting peptide helix/coil equilibrium populations. Protein Sci. 6, 1920-36.
    • (1997) Protein Sci. , vol.6 , pp. 1920-1936
    • Andersen, N.H.1    Tong, H.2
  • 152
    • 0027497118 scopus 로고
    • The energetics of ion-pair and hydrogenbonding interactions in a helical peptide
    • Scholtz, J. M., Qian, H., Robbins, V. H., and Baldwin, R. L. (1993). The energetics of ion-pair and hydrogenbonding interactions in a helical peptide. Biochemistry 32, 9668-76.
    • (1993) Biochemistry , vol.32 , pp. 9668-9676
    • Scholtz, J.M.1    Qian, H.2    Robbins, V.H.3    Baldwin, R.L.4
  • 153
    • 0029023465 scopus 로고
    • Incorporation of pairwise interactions into the Lifson-Roig model for helix prediction
    • Shalongo, W. and Stellwagen, E. (1995). Incorporation of pairwise interactions into the Lifson-Roig model for helix prediction. Protein Sci. 4, 1161-6.
    • (1995) Protein Sci. , vol.4 , pp. 1161-1166
    • Shalongo, W.1    Stellwagen, E.2
  • 154
    • 0020122366 scopus 로고
    • Amino acid distribution in protein secondary structures
    • Argos, P. and Palau, J. (1982). Amino acid distribution in protein secondary structures. Int. J. Pept. Protein Res. 19, 380-93.
    • (1982) Int. J. Pept. Protein Res. , vol.19 , pp. 380-393
    • Argos, P.1    Palau, J.2
  • 155
    • 0032101291 scopus 로고    scopus 로고
    • Dissecting a-helices: position-specific analysis of a-helices in globular proteins
    • Kumar, S. and Bansal, M. (1998). Dissecting a-helices: position-specific analysis of a-helices in globular proteins. Proteins 31, 460-76.
    • (1998) Proteins , vol.31 , pp. 460-476
    • Kumar, S.1    Bansal, M.2
  • 156
    • 0000741864 scopus 로고    scopus 로고
    • Determination of a-helix N1 energies by addition of N1, N2 and N3 preferences to helix-coil theory
    • Sun, J. K., Penel, S., and Doig, A. J. (2000). Determination of a-helix N1 energies by addition of N1, N2 and N3 preferences to helix-coil theory. Protein Sci. 9, 750-4.
    • (2000) Protein Sci. , vol.9 , pp. 750-754
    • Sun, J.K.1    Penel, S.2    Doig, A.J.3
  • 157
    • 0029658119 scopus 로고    scopus 로고
    • Models for the 310-helix/coil, p-helix/coil, and a-helix/310-helix/coil transitions in isolated peptides
    • Rohl, C. A. and Doig, A. J. (1996). Models for the 310-helix/coil, p-helix/coil, and a-helix/310-helix/coil transitions in isolated peptides. Protein Sci. 5, 1687-96.
    • (1996) Protein Sci. , vol.5 , pp. 1687-1696
    • Rohl, C.A.1    Doig, A.J.2
  • 158
    • 0001036213 scopus 로고    scopus 로고
    • Addition of side-chain interactions to 310-helix/coil and a-helix/310-helix/coil theory
    • Sun, J. K. and Doig, A. J. (1998). Addition of side-chain interactions to 310-helix/coil and a-helix/310-helix/coil theory. Protein Sci. 7, 2374-83.
    • (1998) Protein Sci. , vol.7 , pp. 2374-2383
    • Sun, J.K.1    Doig, A.J.2
  • 159
    • 0028447768 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters
    • Muñoz, V. and Serrano, L. (1994). Elucidating the folding problem of helical peptides using empirical parameters. Nat. Struct. Biol. 1, 399-409.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 399-409
    • Muñoz, V.1    Serrano, L.2
  • 160
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of a-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms
    • Muñoz, V. and Serrano, L. (1997). Development of the multiple sequence approximation within the AGADIR model of a-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms. Biopolymers 41, 495-509.
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Muñoz, V.1    Serrano, L.2
  • 162
    • 0032553332 scopus 로고    scopus 로고
    • Elucidating the folding problem of a-helices: local motifs, long-range electrostatics, ionicstrength dependence and prediction of NMR parameters
    • Lacroix, E., Viguera, A. R., and Serrano, L. (1998). Elucidating the folding problem of a-helices: local motifs, long-range electrostatics, ionicstrength dependence and prediction of NMR parameters. J. Mol. Biol. 284, 173-91.
    • (1998) J. Mol. Biol. , vol.284 , pp. 173-191
    • Lacroix, E.1    Viguera, A.R.2    Serrano, L.3
  • 163
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Muñoz, V. and Serrano, L. (1995). Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 245, 275-96.
    • (1995) J. Mol. Biol. , vol.245 , pp. 275-296
    • Muñoz, V.1    Serrano, L.2
  • 164
    • 0032562654 scopus 로고    scopus 로고
    • Position dependence of nonpolar amino acid intrinsic helical propensities
    • Petukhov, M., Muñoz, V., Yumoto, N., Yoshikawa, S., and Serrano, L. (1998). Position dependence of nonpolar amino acid intrinsic helical propensities. J. Mol. Biol. 278, 279-89.
    • (1998) J. Mol. Biol. , vol.278 , pp. 279-289
    • Petukhov, M.1    Muñoz, V.2    Yumoto, N.3    Yoshikawa, S.4    Serrano, L.5
  • 165
    • 0031214521 scopus 로고    scopus 로고
    • Thermodynamic model of secondary structure for a-helical peptides and proteins
    • Lomize, A. L. and Mosberg, H. I. (1997). Thermodynamic model of secondary structure for a-helical peptides and proteins. Biopolymers 42, 239-69.
    • (1997) Biopolymers , vol.42 , pp. 239-269
    • Lomize, A.L.1    Mosberg, H.I.2
  • 166
    • 0023673867 scopus 로고
    • Effect of sequence-specific interactions on the stability of helical conformations in polypeptides
    • Vásquez, M. and Scheraga, H. A. (1988). Effect of sequence-specific interactions on the stability of helical conformations in polypeptides. Biopolymers 27, 41-58.
    • (1988) Biopolymers , vol.27 , pp. 41-58
    • Vásquez, M.1    Scheraga, H.A.2
  • 167
    • 0025043788 scopus 로고
    • A hierarchical nesting approach to describe the stability of a helices with side chain interactions
    • Roberts, C. H. (1990). A hierarchical nesting approach to describe the stability of a helices with side chain interactions. Biopolymers 30, 335-47.
    • (1990) Biopolymers , vol.30 , pp. 335-347
    • Roberts, C.H.1
  • 168
    • 0013817874 scopus 로고
    • The influence of amino acid sequence on protein structure
    • Guzzo, A. V. (1965). The influence of amino acid sequence on protein structure. Biophys. J. 5, 809-22.
    • (1965) Biophys. J. , vol.5 , pp. 809-822
    • Guzzo, A.V.1
  • 169
    • 0000142773 scopus 로고
    • A correlation between amino acid composition and protein structure
    • Davies, D. R. (1964). A correlation between amino acid composition and protein structure. J. Mol. Biol. 9, 605-9.
    • (1964) J. Mol. Biol. , vol.9 , pp. 605-609
    • Davies, D.R.1
  • 170
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, b-sheet and random coil regions calculated from proteins
    • Chou, P. Y. and Fasman, G. D. (1974). Conformational parameters for amino acids in helical, b-sheet and random coil regions calculated from proteins. Biochemistry 13, 211-21.
    • (1974) Biochemistry , vol.13 , pp. 211-221
    • Chou, P.Y.1    Fasman, G.D.2
  • 171
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou, P. Y. and Fasman, G. D. (1978). Empirical predictions of protein conformation. Annu. Rev. Biochem. 47, 251-76.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 172
    • 0000242042 scopus 로고
    • Helix-coil stability constants for the naturally occurring amino acids in water. I. Properties of copolymers and approximate theories
    • Von Dreele, P. H., Poland, D., and Scheraga, H. A. (1971). Helix-coil stability constants for the naturally occurring amino acids in water. I. Properties of copolymers and approximate theories. Macromolecules 4, 396-407.
    • (1971) Macromolecules , vol.4 , pp. 396-407
    • Von Dreele, P.H.1    Poland, D.2    Scheraga, H.A.3
  • 173
    • 0001552548 scopus 로고
    • Helix-coil stability constants for the naturally occurring amino acids in water. II. Characterization of the host polymers and application of the hostguest technique to random poly-(hydroxypropylglutamine-cohydroxybutylglutamine)
    • Von Dreele, P. H., Lotan, N., Ananthanarayanan, V. S., Andreatta, R. H., Poland, D., and Scheraga, H. A. (1971). Helix-coil stability constants for the naturally occurring amino acids in water. II. Characterization of the host polymers and application of the hostguest technique to random poly-(hydroxypropylglutamine-cohydroxybutylglutamine). Macromolecules 4, 408-17.
    • (1971) Macromolecules , vol.4 , pp. 408-417
    • Von Dreele, P.H.1    Lotan, N.2    Ananthanarayanan, V.S.3    Andreatta, R.H.4    Poland, D.5    Scheraga, H.A.6
  • 174
    • 0025113815 scopus 로고
    • Helix-coil stability constants for the naturally occurring amino acids in water. XXIV. Half-cysteine parameters from random poly-(hydroxybutylglutamine-co-Smethylthio-L-cysteine)
    • Wojcik, J., Altmann, K. H., and Scheraga, H. A. (1990). Helix-coil stability constants for the naturally occurring amino acids in water. XXIV. Half-cysteine parameters from random poly-(hydroxybutylglutamine-co-Smethylthio-L-cysteine). Biopolymers 30, 121-34.
    • (1990) Biopolymers , vol.30 , pp. 121-134
    • Wojcik, J.1    Altmann, K.H.2    Scheraga, H.A.3
  • 175
    • 0028142385 scopus 로고
    • Helix-forming tendencies of amino acids in short (hydroxybutyl)-Lglutamine peptides: An evaluation of the contradictory results from hostguest studies and short alanine-based peptides
    • Padmanabhan, S., York, E. J., Gera, L., Stewart, J. M., and Baldwin, R. L. (1994). Helix-forming tendencies of amino acids in short (hydroxybutyl)-Lglutamine peptides: An evaluation of the contradictory results from hostguest studies and short alanine-based peptides. Biochemistry 33, 8604-9.
    • (1994) Biochemistry , vol.33 , pp. 8604-8609
    • Padmanabhan, S.1    York, E.J.2    Gera, L.3    Stewart, J.M.4    Baldwin, R.L.5
  • 176
    • 0028222235 scopus 로고
    • Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions
    • Chakrabartty, A., Kortemme, T., and Baldwin, R. L. (1994). Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Protein Sci. 3, 843-52.
    • (1994) Protein Sci. , vol.3 , pp. 843-852
    • Chakrabartty, A.1    Kortemme, T.2    Baldwin, R.L.3
  • 177
    • 0027236794 scopus 로고
    • Structural basis of amino acid a-helix propensity
    • Blaber, M., Zhang, X.-J., and Matthews, B. W. (1993). Structural basis of amino acid a-helix propensity. Science 260, 1637-40.
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.-J.2    Matthews, B.W.3
  • 178
    • 0027236794 scopus 로고
    • Structural basis of amino acid a-helix propensity
    • Blaber, M. W., Baase, W. A., Gassner, N., and Matthews, B. W. (1993). Structural basis of amino acid a-helix propensity. Science 260, 1637-40.
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.W.1    Baase, W.A.2    Gassner, N.3    Matthews, B.W.4
  • 179
    • 0028178528 scopus 로고
    • Determination of a-helix propensity within the context of a folded protein: sites 44 and 131 in bacteriophage-T4 lysozyme
    • Blaber, M., Zhang, X. J., Lindstrom, J. D., Pepiot, S. D., Baase, W. A., and Matthews, B. W. (1994). Determination of a-helix propensity within the context of a folded protein: sites 44 and 131 in bacteriophage-T4 lysozyme. J. Mol. Biol. 235, 600-24.
    • (1994) J. Mol. Biol. , vol.235 , pp. 600-624
    • Blaber, M.1    Zhang, X.J.2    Lindstrom, J.D.3    Pepiot, S.D.4    Baase, W.A.5    Matthews, B.W.6
  • 180
    • 0026674251 scopus 로고
    • A-Helix stability in proteins. II. Factors that influence stability at an internal position
    • Horovitz, A., Matthews, J. M., and Fersht, A. R. (1992). a-Helix stability in proteins. II. Factors that influence stability at an internal position. J. Mol. Biol. 227, 560-8.
    • (1992) J. Mol. Biol. , vol.227 , pp. 560-568
    • Horovitz, A.1    Matthews, J.M.2    Fersht, A.R.3
  • 181
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil, K. T. and DeGrado, W. F. (1990). A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science 250, 646-51.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 182
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • Pace, C. N. and Scholtz, J. M. (1998). A helix propensity scale based on experimental studies of peptides and proteins. Biophys. J. 75, 422-7.
    • (1998) Biophys. J. , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 184
    • 0034700155 scopus 로고    scopus 로고
    • Physical reasons for the unusual a-helix stabilization afforded by charged or neutral polar residues in alanine-rich peptides
    • Vila, J. A., Ripoll, D. R., and Scheraga, H. A. (2000). Physical reasons for the unusual a-helix stabilization afforded by charged or neutral polar residues in alanine-rich peptides. Proc. Natl Acad. Sci. USA 97, 13075-9.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 13075-13079
    • Vila, J.A.1    Ripoll, D.R.2    Scheraga, H.A.3
  • 185
    • 0033616581 scopus 로고    scopus 로고
    • Alanine is helixstabilizing in both template-nucleated and standard peptide helices
    • Rohl, C. A., Fiori, W., and Baldwin, R. L. (1999). Alanine is helixstabilizing in both template-nucleated and standard peptide helices. Proc. Natl Acad. Sci. USA 96, 3682-7.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3682-3687
    • Rohl, C.A.1    Fiori, W.2    Baldwin, R.L.3
  • 186
    • 0037065689 scopus 로고    scopus 로고
    • Consistent helicities from CD and template t/c data for N-templated polyalanines: progress toward resolution of the alanine helicity problem
    • Kennedy, R. J., Tsang, K.-Y., and Kemp, D. S. (2002). Consistent helicities from CD and template t/c data for N-templated polyalanines: progress toward resolution of the alanine helicity problem. J. Am. Chem. Soc. 124, 934-44.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 934-944
    • Kennedy, R.J.1    Tsang, K.-Y.2    Kemp, D.S.3
  • 187
    • 85023294180 scopus 로고
    • Position-dependent stabilizing effects in a-helices-Nterminal capping in synthetic model peptides
    • Lyu, P. C., Zhou, H. X. X., Jelveh, N., Wemmer, D. E., and Kallenbach, N. R. (1992). Position-dependent stabilizing effects in a-helices-Nterminal capping in synthetic model peptides. J. Am. Chem. Soc. 114, 6560-2.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6560-6562
    • Lyu, P.C.1    Zhou, H.X.X.2    Jelveh, N.3    Wemmer, D.E.4    Kallenbach, N.R.5
  • 188
    • 0032869079 scopus 로고    scopus 로고
    • Position dependence of amino acid intrinsic helical propensities II: Non-charged polar residues: Ser, Thr, Asn, and Gln
    • Petukhov, M., Uegaki, K., Yumoto, N., Yoshikawa, S., and Serrano, L. (1999). Position dependence of amino acid intrinsic helical propensities II: Non-charged polar residues: Ser, Thr, Asn, and Gln. Protein Sci. 8, 2144-50.
    • (1999) Protein Sci. , vol.8 , pp. 2144-2150
    • Petukhov, M.1    Uegaki, K.2    Yumoto, N.3    Yoshikawa, S.4    Serrano, L.5
  • 189
    • 0036127566 scopus 로고    scopus 로고
    • Amino acid intrinsic a-helical propensities III: Positional dependence at several positions of C-terminus
    • Petukhov, M., Uegaki, K., Yumoto, N., and Serrano, L. (2002). Amino acid intrinsic a-helical propensities III: Positional dependence at several positions of C-terminus. Protein Sci. 11, 766-77.
    • (2002) Protein Sci. , vol.11 , pp. 766-777
    • Petukhov, M.1    Uegaki, K.2    Yumoto, N.3    Serrano, L.4
  • 190
    • 0037907569 scopus 로고    scopus 로고
    • Noncharged amino acid residues at the solvent-exposed positions in the middle and at the C terminus of the ahelix have the same helical propensity
    • Ermolenko, D. N., Richardson, J. M., and Makhatadze, G. I. (2003). Noncharged amino acid residues at the solvent-exposed positions in the middle and at the C terminus of the ahelix have the same helical propensity. Protein Sci. 12, 1169-76.
    • (2003) Protein Sci. , vol.12 , pp. 1169-1176
    • Ermolenko, D.N.1    Richardson, J.M.2    Makhatadze, G.I.3
  • 192
    • 0033588864 scopus 로고    scopus 로고
    • A comparison of the a-helix forming propensities and hydrogen bonding properties of serine phosphate and a-amino-gphosphonobutyric acid
    • Liehr, S. and Chenault, H. K. (1999). A comparison of the a-helix forming propensities and hydrogen bonding properties of serine phosphate and a-amino-gphosphonobutyric acid. Bioorg. Med. Chem. Lett. 9, 2759-62.
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 2759-2762
    • Liehr, S.1    Chenault, H.K.2
  • 193
    • 0037065734 scopus 로고    scopus 로고
    • Effect of phosphorylation on a-helix stability as a function of position
    • Andrew, C. D., Warwicker, J., Jones, G. R., and Doig, A. J. (2002). Effect of phosphorylation on a-helix stability as a function of position. Biochemistry 41, 1897-905.
    • (2002) Biochemistry , vol.41 , pp. 1897-1905
    • Andrew, C.D.1    Warwicker, J.2    Jones, G.R.3    Doig, A.J.4
  • 194
    • 0025663105 scopus 로고
    • Strength and co-operativity of contributions of surface salt bridges to protein stability
    • Horovitz, A., Serrano, L., Avron, B., Bycroft, M., and Fersht, A. R. (1990). Strength and co-operativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 216, 1031-44.
    • (1990) J. Mol. Biol. , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 195
    • 0025881752 scopus 로고
    • Effect of amino acid ion pairs on peptide helicity
    • Merutka, G. and Stellwagen, E. (1991). Effect of amino acid ion pairs on peptide helicity. Biochemistry 30, 1591-4.
    • (1991) Biochemistry , vol.30 , pp. 1591-1594
    • Merutka, G.1    Stellwagen, E.2
  • 196
    • 0026926768 scopus 로고
    • The contribution of residue ion pairs to the helical stability of a model peptide
    • Stellwagen, E., Park, S.-H., Shalongo, W., and Jain, A. (1992). The contribution of residue ion pairs to the helical stability of a model peptide. Biopolymers 32, 1193-200.
    • (1992) Biopolymers , vol.32 , pp. 1193-1200
    • Stellwagen, E.1    Park, S.-H.2    Shalongo, W.3    Jain, A.4
  • 197
    • 0027475153 scopus 로고
    • Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacings
    • Huyghues-Despointes, B. M., Scholtz, J. M., and Baldwin, R. L. (1993). Helical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacings. Protein Sci. 2, 80-5.
    • (1993) Protein Sci. , vol.2 , pp. 80-85
    • Huyghues-Despointes, B.M.1    Scholtz, J.M.2    Baldwin, R.L.3
  • 198
    • 0031042074 scopus 로고    scopus 로고
    • Ion-pair and charged hydrogen-bond interactions between histidine and aspartate in a peptide helix
    • Huyghues-Despointes, B. M. and Baldwin, R. L. (1997). Ion-pair and charged hydrogen-bond interactions between histidine and aspartate in a peptide helix. Biochemistry 36, 1965-70.
    • (1997) Biochemistry , vol.36 , pp. 1965-1970
    • Huyghues-Despointes, B.M.1    Baldwin, R.L.2
  • 199
    • 0028882032 scopus 로고
    • Measuring the strength of side-chain hydrogen bonds in peptide helices: the Gln.Asp (i; i {thorn} 4) interaction
    • Huyghues-Despointes, B. M., Klingler, T. M., and Baldwin, R. L. (1995). Measuring the strength of side-chain hydrogen bonds in peptide helices:
    • (1995) Biochemistry , vol.34 , pp. 13267-13271
    • Huyghues-Despointes, B.M.1    Klingler, T.M.2    Baldwin, R.L.3
  • 200
    • 0031587297 scopus 로고    scopus 로고
    • Hydrogen bonding interactions between Glutamine and Asparagine in a-helical peptides
    • Stapley, B. J. and Doig, A. J. (1997). Hydrogen bonding interactions between Glutamine and Asparagine in a-helical peptides. J. Mol. Biol. 272, 465-73.
    • (1997) J. Mol. Biol. , vol.272 , pp. 465-473
    • Stapley, B.J.1    Doig, A.J.2
  • 201
    • 0028569692 scopus 로고
    • Tests for helix-stabilizing interactions between various nonpolar side chains in alanine-based peptides
    • Padmanabhan, S. and Baldwin, R. L. (1994). Tests for helix-stabilizing interactions between various nonpolar side chains in alanine-based peptides. Protein Sci. 3, 1992-7.
    • (1994) Protein Sci. , vol.3 , pp. 1992-1997
    • Padmanabhan, S.1    Baldwin, R.L.2
  • 202
    • 0027968834 scopus 로고
    • Helix-stabilizing interaction between tyrosine and leucine or valine when the spacing is i; i {thorn} 4
    • Padmanabhan, S. and Baldwin, R. L. (1994). Helix-stabilizing interaction between tyrosine and leucine or valine when the spacing is i; i {thorn} 4. J. Mol. Biol. 241, 706-13.
    • (1994) J. Mol. Biol. , vol.241 , pp. 706-713
    • Padmanabhan, S.1    Baldwin, R.L.2
  • 203
    • 0029034436 scopus 로고
    • Side-chain interactions between sulfur-containing amino acids and phenylalanine in a-helices
    • Viguera, A. R. and Serrano, L. (1995). Side-chain interactions between sulfur-containing amino acids and phenylalanine in a-helices. Biochemistry 34, 8771-9.
    • (1995) Biochemistry , vol.34 , pp. 8771-8779
    • Viguera, A.R.1    Serrano, L.2
  • 204
    • 0037132596 scopus 로고    scopus 로고
    • Simple cation-p interaction between a phenyl ring and a protonated amine stabilizes an ahelix in water
    • Tsou, L. K., Tatko, C. D., and Waters, M. L. (2002). Simple cation-p interaction between a phenyl ring and a protonated amine stabilizes an ahelix in water. J. Am. Chem. Soc. 124, 14917-21.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14917-14921
    • Tsou, L.K.1    Tatko, C.D.2    Waters, M.L.3
  • 205
    • 0036388796 scopus 로고    scopus 로고
    • The synthesis and study of side-chain lactam-bridged peptides
    • Taylor, J. W. (2002). The synthesis and study of side-chain lactam-bridged peptides. Biopolymers 66, 49-75.
    • (2002) Biopolymers , vol.66 , pp. 49-75
    • Taylor, J.W.1
  • 206
    • 0028916225 scopus 로고
    • Rational design, synthesis, and biological evaluation of novel growth-hormone releasing-factor analogs
    • Campbell, R. M., Bongers, J., and Felxi, A. M. (1995). Rational design, synthesis, and biological evaluation of novel growth-hormone releasing-factor analogs. Biopolymers 37, 67-8.
    • (1995) Biopolymers , vol.37 , pp. 67-68
    • Campbell, R.M.1    Bongers, J.2    Felxi, A.M.3
  • 207
    • 0025916569 scopus 로고
    • Cyclic parathyroidhormone related protein antagonists-lysine 13 to aspartic acid 17 [I to (I {thorn} 40] side-chain to side-chain lactamization
    • Chorev, M., Roubini, E., McKee, R. L. et al. (1991). Cyclic parathyroidhormone related protein antagonists-lysine 13 to aspartic acid 17 [I to (I {thorn} 40] side-chain to side-chain lactamization. Biochemistry 30, 5968-74.
    • (1991) Biochemistry , vol.30 , pp. 5968-5974
    • Chorev, M.1    Roubini, E.2    McKee, R.L.3
  • 208
    • 0000953716 scopus 로고
    • Multicyclic polypeptide model compounds. 2. Synthesis and conformational properties of a highly a-helical uncosapeptide constrained by 3 side-chain to side-chain lactam bridges
    • Osapay, G. and Taylor, J. W. (1992). Multicyclic polypeptide model compounds. 2. Synthesis and conformational properties of a highly a-helical uncosapeptide constrained by 3 side-chain to side-chain lactam bridges. J. Am. Chem. Soc. 114, 6966-73.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6966-6973
    • Osapay, G.1    Taylor, J.W.2
  • 209
    • 0026517338 scopus 로고
    • Probing the functional conformation of Neuropeptide-T through the design and study of cyclic analogs
    • Bouvier, M. and Taylor, J. W. (1992). Probing the functional conformation of Neuropeptide-T through the design and study of cyclic analogs. J. Med. Chem. 35, 1145-55.
    • (1992) J. Med. Chem. , vol.35 , pp. 1145-1155
    • Bouvier, M.1    Taylor, J.W.2
  • 210
    • 0028956430 scopus 로고
    • Structural and conformational requirements for human calcitonin activity-design, synthesis, and study of lactam-bridged analogs
    • Kapurniotu, A. and Taylor, J. W. (1995). Structural and conformational requirements for human calcitonin activity-design, synthesis, and study of lactam-bridged analogs. J. Med. Chem. 38, 836-47.
    • (1995) J. Med. Chem. , vol.38 , pp. 836-847
    • Kapurniotu, A.1    Taylor, J.W.2
  • 211
    • 0025007537 scopus 로고
    • Multicyclic polypeptide model compounds. 1. Synthesis of a tricyclic amphiphilic a-helical peptide using an oxime resin, segment-condensation approach
    • Osapay, G. and Taylor, J. W. (1990). Multicyclic polypeptide model compounds. 1. Synthesis of a tricyclic amphiphilic a-helical peptide using an oxime resin, segment-condensation approach. J. Am. Chem. Soc. 112, 6046-51.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6046-6051
    • Osapay, G.1    Taylor, J.W.2
  • 212
    • 0000861709 scopus 로고
    • Synthesis and nuclear-magnetic-resonance structure determination of an ahelical, bicyclic, lactam-bridged hexapeptide
    • Bracken, C., Gulyas, J., Taylor, J. W., and Baum, J. (1994). Synthesis and nuclear-magnetic-resonance structure determination of an ahelical, bicyclic, lactam-bridged hexapeptide. J. Am. Chem. Soc. 116, 6431-2.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 6431-6432
    • Bracken, C.1    Gulyas, J.2    Taylor, J.W.3    Baum, J.4
  • 213
    • 0009693601 scopus 로고
    • Facile synthesis of a short peptide with a side-chain-constrained structure
    • Chen, S. T., Chen, H. J., Yu, H. M., and Wang, K. T. (1993). Facile synthesis of a short peptide with a side-chain-constrained structure. J. Chem. Res. (S) 6, 228-9.
    • (1993) J. Chem. Res. (S) , vol.6 , pp. 228-229
    • Chen, S.T.1    Chen, H.J.2    Yu, H.M.3    Wang, K.T.4
  • 214
    • 0029947582 scopus 로고    scopus 로고
    • Efficient solid-phase synthesis of peptides with tripodal side-chain bridges and optimization of the solvent conditions for solid-phase cyclizations
    • Zhang, W. T., and Taylor, J. W. (1996). Efficient solid-phase synthesis of peptides with tripodal side-chain bridges and optimization of the solvent conditions for solid-phase cyclizations. Tetrahedron Lett. 37, 2173-6.
    • (1996) Tetrahedron Lett. , vol.37 , pp. 2173-2176
    • Zhang, W.T.1    Taylor, J.W.2
  • 215
    • 0028139304 scopus 로고
    • Structural and thermodynamic characterization of a bioactive peptide model of apolipoprotein-E-side-chain lactam bridges to constrain the conformation
    • Luo, P. Z., Braddock, D. T., Subramanian, R. M., Meredith, S. C., and Lynn, D. G. (1994). Structural and thermodynamic characterization of a bioactive peptide model of apolipoprotein-E-side-chain lactam bridges to constrain the conformation. Biochemistry 33, 12367-77.
    • (1994) Biochemistry , vol.33 , pp. 12367-12377
    • Luo, P.Z.1    Braddock, D.T.2    Subramanian, R.M.3    Meredith, S.C.4    Lynn, D.G.5
  • 218
    • 0036009333 scopus 로고    scopus 로고
    • Using an azobenzene cross-linker to either increase or decrease peptide helix content upon trans-to-cis photoisomerization
    • Flint, D. G., Kumita, J. R., Smart, O. S., and Wolley, G. A. (2002). Using an azobenzene cross-linker to either increase or decrease peptide helix content upon trans-to-cis photoisomerization. Chem. Biol. 9, 391-7.
    • (2002) Chem. Biol. , vol.9 , pp. 391-397
    • Flint, D.G.1    Kumita, J.R.2    Smart, O.S.3    Wolley, G.A.4
  • 219
    • 0036655377 scopus 로고    scopus 로고
    • Photo-control of peptide helix content by an azobenzene cross-linker: steric interactions with underlying residues are not critical
    • Kumita, J. R., Flint, D. G., Smart, O. S., and Woolley, G. A. (2002). Photo-control of peptide helix content by an azobenzene cross-linker: steric interactions with underlying residues are not critical. Protein Eng. 15, 561-9.
    • (2002) Protein Eng. , vol.15 , pp. 561-569
    • Kumita, J.R.1    Flint, D.G.2    Smart, O.S.3    Woolley, G.A.4
  • 220
    • 0027946254 scopus 로고
    • Helix stop and start signals in peptides and proteins. The capping box does not necessarily prevent helix elongation
    • Jiménez, M. A., Muñoz, V., Rico, M., and Serrano, L. (1994). Helix stop and start signals in peptides and proteins. The capping box does not necessarily prevent helix elongation. J. Mol. Biol. 242, 487-96.
    • (1994) J. Mol. Biol. , vol.242 , pp. 487-496
    • Jiménez, M.A.1    Muñoz, V.2    Rico, M.3    Serrano, L.4
  • 221
    • 0033012736 scopus 로고    scopus 로고
    • C-terminal capping motifs in model helical peptides
    • Kallenbach, N. R. and Gong, Y. X. (1999). C-terminal capping motifs in model helical peptides. Bioorg. Med. Chem. 7, 143-51.
    • (1999) Bioorg. Med. Chem. , vol.7 , pp. 143-151
    • Kallenbach, N.R.1    Gong, Y.X.2
  • 222
    • 0030071921 scopus 로고    scopus 로고
    • Factors that affect the stabilization of a-helices in short peptides by a capping box
    • Petukhov, M., Yumoto, N., Murase, S., Onmura, R., and Yoshikawa, S. (1996). Factors that affect the stabilization of a-helices in short peptides by a capping box. Biochemistry 35, 387-97.
    • (1996) Biochemistry , vol.35 , pp. 387-397
    • Petukhov, M.1    Yumoto, N.2    Murase, S.3    Onmura, R.4    Yoshikawa, S.5
  • 223
    • 0029086158 scopus 로고
    • Experimental analysis of the Schellman motif
    • Viguera, A. R. and Serrano, L. (1995). Experimental analysis of the Schellman motif. J. Mol. Biol. 251, 150-60.
    • (1995) J. Mol. Biol. , vol.251 , pp. 150-160
    • Viguera, A.R.1    Serrano, L.2
  • 224
    • 0029081270 scopus 로고
    • Structural analysis of the N-and C-termini in a peptide with consensus sequence
    • Gong, Y., Zhou, H. X., Guo, M., and Kallenbach, N. R. (1995). Structural analysis of the N-and C-termini in a peptide with consensus sequence. Protein Sci. 4, 1446-56.
    • (1995) Protein Sci. , vol.4 , pp. 1446-1456
    • Gong, Y.1    Zhou, H.X.2    Guo, M.3    Kallenbach, N.R.4
  • 225
    • 0027524623 scopus 로고
    • Charged histidine affects ahelix stability at all positions in the helix by interacting with the backbone charges
    • Armstrong, K. M. and Baldwin, R. L. (1993). Charged histidine affects ahelix stability at all positions in the helix by interacting with the backbone charges. Proc. Natl Acad. Sci. USA 90, 11337-40.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11337-11340
    • Armstrong, K.M.1    Baldwin, R.L.2
  • 226
    • 12044251376 scopus 로고
    • A neutral water-soluble, a-helical peptide: The effect of ionic strength on the helix-coil equilibrium
    • Scholtz, J. M., York, E. J., Stewart, J. M., and Baldwin, R. L. (1991). A neutral water-soluble, a-helical peptide: The effect of ionic strength on the helix-coil equilibrium. J. Am. Chem. Soc. 113, 5102-4.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5102-5104
    • Scholtz, J.M.1    York, E.J.2    Stewart, J.M.3    Baldwin, R.L.4
  • 227
    • 0032488654 scopus 로고    scopus 로고
    • Energetics of polar side-chain interactions in helical peptides: Salt effects on ion pairs and hydrogen bonds
    • Smith, J. S. and Scholtz, J. M. (1998). Energetics of polar side-chain interactions in helical peptides: Salt effects on ion pairs and hydrogen bonds. Biochemistry 37, 33-40.
    • (1998) Biochemistry , vol.37 , pp. 33-40
    • Smith, J.S.1    Scholtz, J.M.2
  • 228
    • 0027912723 scopus 로고
    • Electrostatic screening of charge and dipole interactions with the helix backbone
    • Lockhart, D. J. and Kim, P. S. (1993). Electrostatic screening of charge and dipole interactions with the helix backbone. Science 260, 198-202.
    • (1993) Science , vol.260 , pp. 198-202
    • Lockhart, D.J.1    Kim, P.S.2
  • 229
    • 0345676548 scopus 로고    scopus 로고
    • Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper)
    • Jelesarov, I., Durr, E., Thomas, R. M., and Bosshard, H. B. (1998). Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper). Biochemistry 37, 7539-50.
    • (1998) Biochemistry , vol.37 , pp. 7539-7550
    • Jelesarov, I.1    Durr, E.2    Thomas, R.M.3    Bosshard, H.B.4
  • 230
    • 0025849701 scopus 로고
    • Calorimetric determination of the enthalpy change for the a-helix to coil transition of an alanine peptide in water
    • Scholtz, J. M., Marqusee, S., Baldwin, R. L. et al. (1991). Calorimetric determination of the enthalpy change for the a-helix to coil transition of an alanine peptide in water. Proc. Natl Acad. Sci. USA 88, 2854-8.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2854-2858
    • Scholtz, J.M.1    Marqusee, S.2    Baldwin, R.L.3
  • 231
    • 0030687509 scopus 로고    scopus 로고
    • Characterization of alanine-rich peptides, Ac-(AAKAA)n-GY-NH2 (n) 1-4), using vibrational circular dichroism and fourier transform infrared conformational determination and thermal unfolding
    • Yoder, G., Pancoska, P., and Keiderling, T. A. (1997). Characterization of alanine-rich peptides, Ac-(AAKAA)n-GY-NH2 (n) 1-4), using vibrational circular dichroism and fourier transform infrared conformational determination and thermal unfolding. Biochemistry 36, 5123-33.
    • (1997) Biochemistry , vol.36 , pp. 5123-5133
    • Yoder, G.1    Pancoska, P.2    Keiderling, T.A.3
  • 232
    • 0035955148 scopus 로고    scopus 로고
    • Temperaturedependent helix-coil transition of an alanine based peptide
    • Huang, C. Y., Klemke, J. W., Getahun, Z., DeGrado, W. F., and Gai, F. (2001). Temperaturedependent helix-coil transition of an alanine based peptide. J. Am. Chem. Soc. 123, 9235-8.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9235-9238
    • Huang, C.Y.1    Klemke, J.W.2    Getahun, Z.3    DeGrado, W.F.4    Gai, F.5
  • 234
    • 0022804939 scopus 로고
    • Stabilization of the ribonuclease Speptide a-helix by trifluoroethanol
    • Nelson, J. W. and N. R., K. (1986). Stabilization of the ribonuclease Speptide a-helix by trifluoroethanol. Proteins: Struct. Funct. Genet. 1, 211-17.
    • (1986) Proteins: Struct. Funct. Genet. , vol.1 , pp. 211-217
    • Nelson, J.W.1
  • 235
    • 0024473893 scopus 로고
    • Persistence of the a-helix stop signal in the S-peptide in trifluoroethanol solutions
    • Nelson, J. W. and N. R., K. (1989). Persistence of the a-helix stop signal in the S-peptide in trifluoroethanol solutions. Biochemistry 28, 5256-61.
    • (1989) Biochemistry , vol.28 , pp. 5256-5261
    • Nelson, J.W.1
  • 236
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide
    • Sonnichsen, F. D., Van Eyk, J. E., Hodges, R. S., and Sykes, B. D. (1992). Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry 31, 8790-8.
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sonnichsen, F.D.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 237
    • 0028279006 scopus 로고
    • Importance of environment in determining secondary structure in proteins
    • Waterhous, D. V. and Johnson, W. C. (1994). Importance of environment in determining secondary structure in proteins. Biochemistry 33, 2121-8.
    • (1994) Biochemistry , vol.33 , pp. 2121-2128
    • Waterhous, D.V.1    Johnson, W.C.2
  • 238
    • 0028174643 scopus 로고
    • Quantitative determination of helical propensities. Analysis of data from trifluoroethanol titration curves
    • Jasanoff, A. and Fersht, A. R. (1984). Quantitative determination of helical propensities. Analysis of data from trifluoroethanol titration curves. Biochemistry 33, 2129-35.
    • (1984) Biochemistry , vol.33 , pp. 2129-2135
    • Jasanoff, A.1    Fersht, A.R.2
  • 239
    • 0028951041 scopus 로고
    • Stabilization of helical domains in short peptides using hydrophobic interactions
    • Albert, J. S. and Hamilton, A. D. (1995). Stabilization of helical domains in short peptides using hydrophobic interactions. Biochemistry 34, 984-90.
    • (1995) Biochemistry , vol.34 , pp. 984-990
    • Albert, J.S.1    Hamilton, A.D.2
  • 240
    • 0032572054 scopus 로고    scopus 로고
    • An indirect chaotropic mechanism for the stabilization of helix conformation of peptides in aqueous trifluoroethanol and hexafluoro-2-propanol
    • Walgers, R., Lee, T. C., and Cammers-Goodwin, A. (1998). An indirect chaotropic mechanism for the stabilization of helix conformation of peptides in aqueous trifluoroethanol and hexafluoro-2-propanol. J. Am. Chem. Soc. 120, 5073-9.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5073-5079
    • Walgers, R.1    Lee, T.C.2    Cammers-Goodwin, A.3
  • 241
    • 0033608974 scopus 로고    scopus 로고
    • Interaction between water and polar groups of the helix backbone: An important determinant of helix propensities
    • Luo, P. and Baldwin, R. L. (1999). Interaction between water and polar groups of the helix backbone: An important determinant of helix propensities. Proc. Natl Acad. Sci. USA 96, 4930-5.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4930-4935
    • Luo, P.1    Baldwin, R.L.2
  • 242
    • 0032514771 scopus 로고    scopus 로고
    • Trifluoroethanol promotes helix formation by destabilizing backbone exposure: Desolvation rather than native hydrogen bonding defines the kinetic pathway of dimeric coiled coil folding
    • Kentsis, A. and Sosnick, T. R. (1998). Trifluoroethanol promotes helix formation by destabilizing backbone exposure: Desolvation rather than native hydrogen bonding defines the kinetic pathway of dimeric coiled coil folding. Biochemistry 37, 14613-22.
    • (1998) Biochemistry , vol.37 , pp. 14613-14622
    • Kentsis, A.1    Sosnick, T.R.2
  • 243
    • 0034493728 scopus 로고    scopus 로고
    • Trifluoroethanol may form a solvent matrix for assisted hydrophobic interactions between peptide sidechains
    • Reiersen, H. and Rees, A. R. (2000). Trifluoroethanol may form a solvent matrix for assisted hydrophobic interactions between peptide sidechains. Protein Eng. 13, 739-43.
    • (2000) Protein Eng. , vol.13 , pp. 739-743
    • Reiersen, H.1    Rees, A.R.2
  • 244
    • 0031889226 scopus 로고    scopus 로고
    • Trifluoroethanol effects on helix propensity and electrostatic interactions in the helical peptide from ribonuclease T1
    • Myers, J. K., Pace, N., and Scholtz, J. M. (1998). Trifluoroethanol effects on helix propensity and electrostatic interactions in the helical peptide from ribonuclease T1. Protein Sci. 7, 383-8.
    • (1998) Protein Sci. , vol.7 , pp. 383-388
    • Myers, J.K.1    Pace, N.2    Scholtz, J.M.3
  • 245
    • 0014217191 scopus 로고
    • Intrinsic dissociation constants of aspartyl and glutamyl carboxyl groups
    • Nozaki, Y. and Tanford, C. (1967). Intrinsic dissociation constants of aspartyl and glutamyl carboxyl groups. J. Biol. Chem. 242, 4731-5.
    • (1967) J. Biol. Chem. , vol.242 , pp. 4731-4735
    • Nozaki, Y.1    Tanford, C.2
  • 246
    • 0004241543 scopus 로고
    • Structure in Protein Chemistry
    • Garland Publishing, New York and London
    • Kyte, J. (1995). Structure in Protein Chemistry, Garland Publishing, New York and London.
    • (1995)
    • Kyte, J.1
  • 247
    • 0028886558 scopus 로고
    • Ionisation of cysteine residues at the termini of model a-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family
    • Kortemme, T. and Creighton, T. E. (1995). Ionisation of cysteine residues at the termini of model a-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family. J. Mol. Biol. 253, 799-812.
    • (1995) J. Mol. Biol. , vol.253 , pp. 799-812
    • Kortemme, T.1    Creighton, T.E.2
  • 248
    • 0037215326 scopus 로고    scopus 로고
    • Positiondependent interactions between cysteine and the helix dipole
    • Miranda, J. J. (2003). Positiondependent interactions between cysteine and the helix dipole. Protein Sci. 12, 73-81.
    • (2003) Protein Sci. , vol.12 , pp. 73-81
    • Miranda, J.J.1
  • 249
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: a measure of the amphiphilicity of a helix
    • Eisenberg, D., Weiss, R. M., and Terwilliger, T. C. (1982). The helical hydrophobic moment: a measure of the amphiphilicity of a helix. Nature 299, 371-4.
    • (1982) Nature , vol.299 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 250
    • 20744456789 scopus 로고
    • Solid phase peptide synthesis. I. The synthesis of a tetrapeptide
    • Merrifield, R. B. (1963). Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. J. Am. Chem. Soc. 85, 2149-54.
    • (1963) J. Am. Chem. Soc. , vol.85 , pp. 2149-2154
    • Merrifield, R.B.1
  • 251
    • 0003714939 scopus 로고    scopus 로고
    • Fmoc solid phase peptide synthesis
    • A practical approach (Hames, B. D., ed.), pp. 9-40. Oxford University Press, Oxford
    • White, P. D. and Chan, W. C. (2000). Fmoc solid phase peptide synthesis. A practical approach (Hames, B. D., ed.), pp. 9-40. Oxford University Press, Oxford.
    • (2000)
    • White, P.D.1    Chan, W.C.2
  • 252
    • 2142752826 scopus 로고
    • The 9-fluorenylmethoxycarbonyl function, a new base-sensitive aminoprotecting group
    • Carpino, L. A. and Han, G. Y. (1970). The 9-fluorenylmethoxycarbonyl function, a new base-sensitive aminoprotecting group. J. Am. Chem. Soc. 92, 5748-9.
    • (1970) J. Am. Chem. Soc. , vol.92 , pp. 5748-5749
    • Carpino, L.A.1    Han, G.Y.2
  • 253
    • 33947091567 scopus 로고
    • The 9-fluorenylmethoxycarbonyl amino-protecting group
    • Carpino, L. A. and Han, G. Y. (1972). The 9-fluorenylmethoxycarbonyl amino-protecting group. J. Org. Chem. 37, 3404-9.
    • (1972) J. Org. Chem. , vol.37 , pp. 3404-3409
    • Carpino, L.A.1    Han, G.Y.2
  • 254
    • 0014772602 scopus 로고
    • Color test for detection of free terminal amino groups in the solidphase synthesis of peptide
    • Kaiser, E., Colescott, R. L., Bossinger, C. D., and Cook, P. I. (1970). Color test for detection of free terminal amino groups in the solidphase synthesis of peptide. Anal. Biochem. 34, 595-8.
    • (1970) Anal. Biochem. , vol.34 , pp. 595-598
    • Kaiser, E.1    Colescott, R.L.2    Bossinger, C.D.3    Cook, P.I.4
  • 255
    • 0019627519 scopus 로고
    • Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction
    • Sarin, V. K., Kent, S. B. H., Tam, J. P., and Merrifield, R. B. (1981). Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction. Anal. Biochem. 117, 147-57.
    • (1981) Anal. Biochem. , vol.117 , pp. 147-157
    • Sarin, V.K.1    Kent, S.B.H.2    Tam, J.P.3    Merrifield, R.B.4
  • 256
    • 0030042763 scopus 로고    scopus 로고
    • Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
    • Greenfield, N. J. (1996). Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. Biochemistry 235, 1-10.
    • (1996) Biochemistry , vol.235 , pp. 1-10
    • Greenfield, N.J.1
  • 257
    • 0001837510 scopus 로고
    • ACS Symposium Series
    • OUP, New York
    • Manning, M. C. (1993). ACS Symposium Series, Vol. 516, pp. 33-52, OUP, New York.
    • (1993) , vol.516 , pp. 33-52
    • Manning, M.C.1
  • 258
    • 0003786121 scopus 로고    scopus 로고
    • Circular Dichroism and the Conformational Analysis of Biomolecules
    • Plenum Press, New York
    • Fasman, G. D. (1996). Circular Dichroism and the Conformational Analysis of Biomolecules. Plenum Press, New York.
    • (1996)
    • Fasman, G.D.1
  • 259
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water
    • Luo, P. and Baldwin, R. L. (1997). Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry 36, 8413-21.
    • (1997) Biochemistry , vol.36 , pp. 8413-8421
    • Luo, P.1    Baldwin, R.L.2
  • 260
    • 0015997959 scopus 로고
    • Thermodynamics and dynamics of histidine-binding protein, the watersoluble receptor of histidine permease
    • Strickland, E. H. (1974). Thermodynamics and dynamics of histidine-binding protein, the watersoluble receptor of histidine permease. CRC Crit. Rev. Biochem. 2, 113-74.
    • (1974) CRC Crit. Rev. Biochem. , vol.2 , pp. 113-174
    • Strickland, E.H.1
  • 261
    • 0024464461 scopus 로고
    • Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor
    • Manning, M. C. and Woody, R. W. (1989). Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor. Biochemistry 28, 8609-13.
    • (1989) Biochemistry , vol.28 , pp. 8609-8613
    • Manning, M.C.1    Woody, R.W.2
  • 262
    • 0002364711 scopus 로고    scopus 로고
    • In Circular Dichroism and the Conformational Analysis of Biomolecules
    • (Fasman, G. D., ed.), Plenum Press, New York
    • Woody, R. W., Dunker, A. K., and Fasman, G. D. (1996). In Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G. D., ed.), pp. 109-157. Plenum Press, New York.
    • (1996) , pp. 109-157
    • Woody, R.W.1    Dunker, A.K.2    Fasman, G.D.3
  • 263
    • 0014448179 scopus 로고
    • The rotatory properties of molecules containing two peptide groups
    • Bayley, P. M., Nielsen, E. B., and Schellman, J. A. (1969). The rotatory properties of molecules containing two peptide groups. J. Phys. Chem. 73, 228-43.
    • (1969) J. Phys. Chem. , vol.73 , pp. 228-243
    • Bayley, P.M.1    Nielsen, E.B.2    Schellman, J.A.3
  • 264
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama, N. and Woody, R. W. (1993). A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209, 32-44.
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 265
    • 0036802313 scopus 로고    scopus 로고
    • Protein and peptide secondary structure and conformational determination with vibrational circular dichroism
    • Keiderling, T. A. (2002). Protein and peptide secondary structure and conformational determination with vibrational circular dichroism. Curr. Opin. Struct. Biol. 6, 682-8.
    • (2002) Curr. Opin. Struct. Biol. , vol.6 , pp. 682-688
    • Keiderling, T.A.1
  • 266
    • 0000042757 scopus 로고    scopus 로고
    • In Circular Dichroism: Principles and Applications
    • (Berova, N., Nakanishi, K., and Woody, R. A., eds), Wiley-VCH, New York
    • Keiderling, T. A. (2002). In Circular Dichroism: Principles and Applications (Berova, N., Nakanishi, K., and Woody, R. A., eds), pp. 621-666. Wiley-VCH, New York.
    • (2002) , pp. 621-666
    • Keiderling, T.A.1
  • 267
    • 0034972835 scopus 로고    scopus 로고
    • Conformational study on poly[g-(a-phenethyl)-Lglutamate] using vibrational circular dichroism spectroscopy
    • Tanaka, T., Inoue, K., Kodama, T., Kyogoku, Y., Hayakawa, T., and Sugeta, H. (2001). Conformational study on poly[g-(a-phenethyl)-Lglutamate] using vibrational circular dichroism spectroscopy. Biopolymers 62, 228-34.
    • (2001) Biopolymers , vol.62 , pp. 228-234
    • Tanaka, T.1    Inoue, K.2    Kodama, T.3    Kyogoku, Y.4    Hayakawa, T.5    Sugeta, H.6
  • 268
    • 0030596499 scopus 로고    scopus 로고
    • Predictions of secondary structure using statistical analyses of electronic and vibrational circular dichroism and Fourier transform infrared spectra of proteins in H2O
    • Baumruk, V., Pancoska, P., and Keiderling, T. A. (1996). Predictions of secondary structure using statistical analyses of electronic and vibrational circular dichroism and Fourier transform infrared spectra of proteins in H2O. J. Mol. Biol. 259, 774-91.
    • (1996) J. Mol. Biol. , vol.259 , pp. 774-791
    • Baumruk, V.1    Pancoska, P.2    Keiderling, T.A.3
  • 269
    • 0034317389 scopus 로고    scopus 로고
    • Dual polarization modulation: a real-time, spectral multiplex separation of circular dichroism from linear birefringence spectral intensities
    • Nafie, L. A. (2000). Dual polarization modulation: a real-time, spectral multiplex separation of circular dichroism from linear birefringence spectral intensities. Appl. Spectros. 54, 1634-45.
    • (2000) Appl. Spectros. , vol.54 , pp. 1634-1645
    • Nafie, L.A.1
  • 270
    • 0035508358 scopus 로고    scopus 로고
    • Polarization modulation Fourier transform infrared spectroscopy with digital signal processing: comparison of vibrational circular dichroism method
    • Hilario, J., Drapcho, D., Curbelo, R., and Keiderling, T. A. (2001). Polarization modulation Fourier transform infrared spectroscopy with digital signal processing: comparison of vibrational circular dichroism method. Appl. Spectros. 55, 1435-47.
    • (2001) Appl. Spectros. , vol.55 , pp. 1435-1447
    • Hilario, J.1    Drapcho, D.2    Curbelo, R.3    Keiderling, T.A.4
  • 271
    • 0030874298 scopus 로고    scopus 로고
    • Comparison of NH exchange and circular dichroism as techniques for measuring the parameters of the helix-coil transition in peptides
    • Rohl, C. A. and Baldwin, R. L. (1997). Comparison of NH exchange and circular dichroism as techniques for measuring the parameters of the helix-coil transition in peptides. Biochemistry 36, 8435-42.
    • (1997) Biochemistry , vol.36 , pp. 8435-8442
    • Rohl, C.A.1    Baldwin, R.L.2
  • 272
    • 0347610773 scopus 로고
    • Empirical correlation between protein backbone conformation and Ca and Cb 13C nuclear magnetic resonance chemical shifts
    • Spera, S. and Bax, A. (1991). Empirical correlation between protein backbone conformation and Ca and Cb 13C nuclear magnetic resonance chemical shifts. J. Am. Chem. Soc. 113, 5490-2.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 273
    • 0001358187 scopus 로고
    • Distribution of helicity within the model peptide Acetyl(AAQAA)3 amide
    • Shalongo, W., Dugad, L., and Stellwagen, E. (1994). Distribution of helicity within the model peptide Acetyl(AAQAA)3 amide. J. Am. Chem. Soc. 116, 8288-93.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8288-8293
    • Shalongo, W.1    Dugad, L.2    Stellwagen, E.3
  • 274
    • 0027975528 scopus 로고
    • Analysis of the thermal transitions of a model helical peptides using C-13 NMR
    • Shalongo, W., Dugad, L., and Stellwagen, E. (1994). Analysis of the thermal transitions of a model helical peptides using C-13 NMR. J. Am. Chem. Soc. 116, 2500-7.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 2500-2507
    • Shalongo, W.1    Dugad, L.2    Stellwagen, E.3
  • 275
    • 0031670005 scopus 로고    scopus 로고
    • Analysis of Nterminal Capping using carbonylcarbon chemical shift measurements
    • Park, S.-H., Shalongo, W., and Stellwagen, E. (1998). Analysis of Nterminal Capping using carbonylcarbon chemical shift measurements. Proteins: Struct. Funct. Genet. 33, 167-76.
    • (1998) Proteins: Struct. Funct. Genet. , vol.33 , pp. 167-176
    • Park, S.-H.1    Shalongo, W.2    Stellwagen, E.3
  • 276
    • 0003919736 scopus 로고
    • NMR of Proteins and Nucleic Acids
    • John Wiley and Sons, New York
    • Wuthrich, K. (1986). NMR of Proteins and Nucleic Acids, John Wiley and Sons, New York.
    • (1986)
    • Wuthrich, K.1
  • 277
    • 0028951155 scopus 로고
    • Nuclear magnetic resonance assignments and secondary structure of bovine S100b protein
    • Kilby, P. M., van Eldick, L. J., and Roberts, G. C. K. (1995). Nuclear magnetic resonance assignments and secondary structure of bovine S100b protein. FEBS Lett. 363, 90-6.
    • (1995) FEBS Lett. , vol.363 , pp. 90-96
    • Kilby, P.M.1    Van Eldick, L.J.2    Roberts, G.C.K.3
  • 278
    • 0004106235 scopus 로고
    • Biological Spectroscopy
    • Benjamin Cummings, Menlo Park, CA
    • Campbell, I. D. and Dwek, R. A. (1984). Biological Spectroscopy. Benjamin Cummings, Menlo Park, CA.
    • (1984)
    • Campbell, I.D.1    Dwek, R.A.2
  • 279
    • 0003573490 scopus 로고
    • Physical Chemistry and its Biological Applications
    • Academic Press, New York
    • Brey, W. S. (1984). Physical Chemistry and its Biological Applications. Academic Press, New York.
    • (1984)
    • Brey, W.S.1
  • 280
    • 0025613794 scopus 로고
    • Quantitative IR Spectrophotometry of peptide compounds in water (H2O) solutions. 2. Amide absorption-bands of polypeptides and fibrous proteins in a-coil, b-coil, and random coil conformations
    • Venyaminov, S.-Y. and Kalnin, N. N. (1990). Quantitative IR Spectrophotometry of peptide compounds in water (H2O) solutions. 2. Amide absorption-bands of polypeptides and fibrous proteins in a-coil, b-coil, and random coil conformations. Biopolymers 30, 1243-57.
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.-Y.1    Kalnin, N.N.2
  • 281
    • 0014199524 scopus 로고
    • Infra-red spectrum and protein conformations in aqueous solutions
    • Susi, H., Timasheff, S. N., and Stevens, L. (1967). Infra-red spectrum and protein conformations in aqueous solutions. J. Biol. Chem. 242, 5460-6.
    • (1967) J. Biol. Chem. , vol.242 , pp. 5460-5466
    • Susi, H.1    Timasheff, S.N.2    Stevens, L.3
  • 282
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides and protein
    • Krimm, S. and Bandekar, J. (1986). Vibrational spectroscopy and conformation of peptides, polypeptides and protein. Adv. Protein Chem. 38, 181-364.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 283
    • 0017250408 scopus 로고
    • Infrared spectra and resonance interactions of amide-I and II vibration of a-helix
    • Nevskaya, N. A. and Chirgadze, Y. N. (1976). Infrared spectra and resonance interactions of amide-I and II vibration of a-helix. Biopolymers 15, 637-48.
    • (1976) Biopolymers , vol.15 , pp. 637-648
    • Nevskaya, N.A.1    Chirgadze, Y.N.2
  • 284
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler, D. M. and Susi, H. (1986). Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25, 469-87.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 285
    • 0022024822 scopus 로고
    • Protein Conformation by Infra-red spectroscopy-Resolution enhancement by Fourier self deconvolution
    • Yang, W.-J., Griffiths, P. R., Byler, D. M., and Susi, H. (1985). Protein Conformation by Infra-red spectroscopy-Resolution enhancement by Fourier self deconvolution. Appl. Spectros. 39, 282-7.
    • (1985) Appl. Spectros. , vol.39 , pp. 282-287
    • Yang, W.-J.1    Griffiths, P.R.2    Byler, D.M.3    Susi, H.4
  • 286
    • 0024053634 scopus 로고
    • Fourier deconvolution of the Amide-I Raman band of proteins as related to conformation
    • Susi, H. and Byler, D. M. (1988). Fourier deconvolution of the Amide-I Raman band of proteins as related to conformation. Appl. Spectros. 42, 819-25.
    • (1988) Appl. Spectros. , vol.42 , pp. 819-825
    • Susi, H.1    Byler, D.M.2
  • 287
    • 0023385638 scopus 로고
    • Quantitative estimation of a-helix coil content in bovine sreum albumin by Fourier transform-infrared spectroscopy
    • Kato, K., Matsui, T., and Tanaka, S. (1987). Quantitative estimation of a-helix coil content in bovine sreum albumin by Fourier transform-infrared spectroscopy. Appl. Spectros. 41, 861-5.
    • (1987) Appl. Spectros. , vol.41 , pp. 861-865
    • Kato, K.1    Matsui, T.2    Tanaka, S.3
  • 288
    • 0013348347 scopus 로고
    • A new type of secondary radiation
    • Raman, C. V. and Krishnan, K. S. (1928). A new type of secondary radiation. Nature 121, 501-2.
    • (1928) Nature , vol.121 , pp. 501-502
    • Raman, C.V.1    Krishnan, K.S.2
  • 289
    • 0004036242 scopus 로고
    • Fourier Transform Raman Spectroscopy
    • Ellis Horwood, Chichester
    • Hendra, P. J., Jones, C., and Warnes, G. (1991). Fourier Transform Raman Spectroscopy. Ellis Horwood, Chichester.
    • (1991)
    • Hendra, P.J.1    Jones, C.2    Warnes, G.3
  • 290
    • 0001876807 scopus 로고    scopus 로고
    • Raman difference studies of protein structure and folding, enzymatic catalysis and ligand binding
    • Callender, R., Deng, H., and Gilmanshin, R. (1998). Raman difference studies of protein structure and folding, enzymatic catalysis and ligand binding. J. Raman Spectros. 29, 15.
    • (1998) J. Raman Spectros. , vol.29 , pp. 15
    • Callender, R.1    Deng, H.2    Gilmanshin, R.3
  • 291
    • 0142229713 scopus 로고    scopus 로고
    • Protein-Ligand Interactions: structure and spectroscopy
    • (Harding, S. E. and Chowdhry, B. Z., eds). Oxford University Press, Oxford
    • Withnall, R. (2001). Protein-Ligand Interactions: structure and spectroscopy (Harding, S. E. and Chowdhry, B. Z., eds). Oxford University Press, Oxford.
    • (2001)
    • Withnall, R.1
  • 292
    • 84889784294 scopus 로고
    • Vibrational Spectra: Principles and Aplications with Emphasis on Optical Activity
    • Methods in Enzymology (Sauer, K., ed.). Academic Press, New York
    • Peticolas, W. L., ed. (1995). Vibrational Spectra: Principles and Aplications with Emphasis on Optical Activity. Vol. 246. Methods in Enzymology (Sauer, K., ed.). Academic Press, New York.
    • (1995) , vol.246
    • Peticolas, W.L.1
  • 293
    • 0035965724 scopus 로고    scopus 로고
    • Dihedral c angle dependence of the amide III vibration: A uniquely sensitive UV resonance Raman secondary structural probe
    • Asher, S. A., Ianoul, A., Mix, G., Boyden, M. N., Karnoup, A., Diem, M., and Schweitzer-Stenner, R. (2001). Dihedral c angle dependence of the amide III vibration: A uniquely sensitive UV resonance Raman secondary structural probe. J. Am. Chem. Soc. 123, 11775-81.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11775-11781
    • Asher, S.A.1    Ianoul, A.2    Mix, G.3    Boyden, M.N.4    Karnoup, A.5    Diem, M.6    Schweitzer-Stenner, R.7
  • 294
    • 0003778871 scopus 로고    scopus 로고
    • Vibrational Spectra: Principles and Applications with Emphasis on Optical Activity
    • Elsevier, Amsterdam
    • Polavarapu, P. L. (1998). Vibrational Spectra: Principles and Applications with Emphasis on Optical Activity. Elsevier, Amsterdam.
    • (1998)
    • Polavarapu, P.L.1
  • 295
    • 0030628997 scopus 로고    scopus 로고
    • Infrared and Raman vibrational optical activity: Theoretical and experimental aspect
    • Nafie, L. A. (1997). Infrared and Raman vibrational optical activity: Theoretical and experimental aspect. Annu. Rev. Phys. Chem. 48, 357-86.
    • (1997) Annu. Rev. Phys. Chem. , vol.48 , pp. 357-386
    • Nafie, L.A.1
  • 296
    • 0028184694 scopus 로고
    • Vibrational Raman optical-activity of alanyl peptide oligomers-a new perspective on aqueous-solution conformation
    • Ford, S. J., Wen, Z. Q., Hecht, L., and Barron, L. D. (1994). Vibrational Raman optical-activity of alanyl peptide oligomers-a new perspective on aqueous-solution conformation. Biopolymers 34, 303-13.
    • (1994) Biopolymers , vol.34 , pp. 303-313
    • Ford, S.J.1    Wen, Z.Q.2    Hecht, L.3    Barron, L.D.4
  • 297
    • 0003819245 scopus 로고
    • Introduction to Modern Vibrational Spectroscopy
    • Wiley, New York
    • Diem, M. (1993). Introduction to Modern Vibrational Spectroscopy, Wiley, New York.
    • (1993)
    • Diem, M.1
  • 298
    • 0028820601 scopus 로고
    • Analysis of i; i {thorn} 5 and i; i {thorn} 8 hydrophobic interactions in a helical model peptide bearing the hydrophobic staple motif
    • Muñoz, V. and Serrano, L. (1995). Analysis of i; i {thorn} 5 and i; i {thorn} 8 hydrophobic interactions in a helical model peptide bearing the hydrophobic staple motif. Biochemistry 34, 15301-6.
    • (1995) Biochemistry , vol.34 , pp. 15301-15306
    • Muñoz, V.1    Serrano, L.2
  • 299
    • 0035845493 scopus 로고    scopus 로고
    • Hydration of the peptide backbone largely defines the thermodynamic propensity scale of residues at the C0 position of the C-capping box of a-helices
    • Thomas, S. T., Loladze, V. V., and Makhatadze, G. I. (2001). Hydration of the peptide backbone largely defines the thermodynamic propensity scale of residues at the C0 position of the C-capping box of a-helices. Proc. Natl Acad. Sci. USA 98, 10670-5.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10670-10675
    • Thomas, S.T.1    Loladze, V.V.2    Makhatadze, G.I.3
  • 300
    • 0037059067 scopus 로고    scopus 로고
    • Nonclassical helix-stabilizing interactions: CaH...O H-bonding between Phe and Glu side chains in a-helical peptides
    • Shi, Z., Olson, C. A., Bell, A. J., and Kallenbach, N. R. (2002). Nonclassical helix-stabilizing interactions: CaH...O H-bonding between Phe and Glu side chains in a-helical peptides. Biophys. Chem. 101-2, 267-79.
    • (2002) Biophys. Chem. , vol.101-102 , pp. 267-279
    • Shi, Z.1    Olson, C.A.2    Bell, A.J.3    Kallenbach, N.R.4
  • 302
    • 0028574137 scopus 로고
    • Contributions of a hydrogen bond/salt bridge network to the stability of secondary and tertiary structure in lambda repressor
    • Marqusee, S. and Sauer, R. T. (1994). Contributions of a hydrogen bond/salt bridge network to the stability of secondary and tertiary structure in lambda repressor. Protein Sci. 3, 2217-25.
    • (1994) Protein Sci. , vol.3 , pp. 2217-2225
    • Marqusee, S.1    Sauer, R.T.2
  • 303
    • 0035746132 scopus 로고    scopus 로고
    • Stabilization of a-helix structure by polar side-chain interactions: Complex salt bridges, cation p interactions and CaH...OaH bonds
    • Shi, Z., Olson, C. A., Bell, A. J., and Kallenbach, N. R. (2001). Stabilization of a-helix structure by polar side-chain interactions: Complex salt bridges, cation p interactions and CaH...OaH bonds. Biopolymers 60, 366-80.
    • (2001) Biopolymers , vol.60 , pp. 366-380
    • Shi, Z.1    Olson, C.A.2    Bell, A.J.3    Kallenbach, N.R.4


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