메뉴 건너뛰기




Volumn 8, Issue 10, 1999, Pages 2144-2150

Position dependence of amino acid intrinsic helical propensities II: Non-charged polar residues: Ser, Thr, Asn, and Gln

Author keywords

Entropy; Folding; Hydration; Secondary structure; Stability; helix

Indexed keywords

ASPARAGINE; GLYCINE; SERINE; THREONINE;

EID: 0032869079     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.10.2144     Document Type: Article
Times cited : (48)

References (30)
  • 1
    • 0028960071 scopus 로고
    • Role of electrostatic screening in determining protein main chain conformational preferences
    • Avbelj F, Moult J. 1995. Role of electrostatic screening in determining protein main chain conformational preferences. Biochemistry 34:755-764.
    • (1995) Biochemistry , vol.34 , pp. 755-764
    • Avbelj, F.1    Moult, J.2
  • 2
    • 0026696173 scopus 로고
    • Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59
    • Bell JA, Becktel WJ, Sauer U, Baase WA, Matthews BW. 1992. Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59. Biochemistry 31:3590-3596.
    • (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
  • 4
    • 0027236794 scopus 로고
    • Structural basis of amino acid alpha helix propensity
    • Blaber M, Zhang XJ, Matthews BW. 1993. Structural basis of amino acid alpha helix propensity. Science 260:1637-1640.
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.J.2    Matthews, B.W.3
  • 5
    • 0025752606 scopus 로고
    • Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an alpha-helical region of carboxypeptidase A
    • Bruch MD, Dhingra MM, Gierasch LM. 1991. Side chain-backbone hydrogen bonding contributes to helix stability in peptides derived from an alpha-helical region of carboxypeptidase A. Proteins 10:130-139.
    • (1991) Proteins , vol.10 , pp. 130-139
    • Bruch, M.D.1    Dhingra, M.M.2    Gierasch, L.M.3
  • 7
    • 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, Baldwin RL. 1993. Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities. Biochemistry 32:5560-5565.
    • (1993) Biochemistry , vol.32 , pp. 5560-5565
    • Chakrabartty, A.1    Kortemme, T.2    Padmanabhan, S.3    Baldwin, R.L.4
  • 8
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Chen YH, Yang JT, Chau KH. 1974. Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry 13: 3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 9
    • 0028178865 scopus 로고
    • Alpha-helix-forming propensities in peptides and proteins
    • Creamer TP, Rose GD. 1994. Alpha-helix-forming propensities in peptides and proteins. Proteins 19:85-97.
    • (1994) Proteins , vol.19 , pp. 85-97
    • Creamer, T.P.1    Rose, G.D.2
  • 10
    • 0029153215 scopus 로고
    • Peptides in membranes: Helicity and hydrophobicity
    • Deber CM, Li SC. 1995. Peptides in membranes: Helicity and hydrophobicity. Biopolymers 37:295-318.
    • (1995) Biopolymers , vol.37 , pp. 295-318
    • Deber, C.M.1    Li, S.C.2
  • 11
    • 0029020484 scopus 로고
    • N- and C-capping preferences for all 20 amino acids in alpha-helical peptides
    • Doig AJ, Baldwin RL. 1995. N- and C-capping preferences for all 20 amino acids in alpha-helical peptides. Protein Sci 4:1325-1336.
    • (1995) Protein Sci , vol.4 , pp. 1325-1336
    • Doig, A.J.1    Baldwin, R.L.2
  • 12
    • 84986483798 scopus 로고
    • The double cubic lattice method: Efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies
    • Eisenhaber F, Lijnzaad P, Argos P, Sander C, Scharf M. 1995. The double cubic lattice method: Efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies. J Comput Chem 16:273-284.
    • (1995) J Comput Chem , vol.16 , pp. 273-284
    • Eisenhaber, F.1    Lijnzaad, P.2    Argos, P.3    Sander, C.4    Scharf, M.5
  • 13
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182:319-326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 14
    • 0028818570 scopus 로고
    • Comparison of atomic solvation parametric sets: Applicability and limitations in protein folding and binding
    • Juffer AH, Eisenhaber F, Hubbard SJ, Walther D, Argos P. 1995. Comparison of atomic solvation parametric sets: Applicability and limitations in protein folding and binding. Protein Sci 4:2499-2509.
    • (1995) Protein Sci , vol.4 , pp. 2499-2509
    • Juffer, A.H.1    Eisenhaber, F.2    Hubbard, S.J.3    Walther, D.4    Argos, P.5
  • 15
    • 0032553332 scopus 로고    scopus 로고
    • Elucidating the folding problem of alpha-helices: Local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters
    • Lacroix E, Viguera AR, Serrano L. 1998. Elucidating the folding problem of alpha-helices: Local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters. J Mol Biol 284:173-191.
    • (1998) J Mol Biol , vol.284 , pp. 173-191
    • Lacroix, E.1    Viguera, A.R.2    Serrano, L.3
  • 16
    • 0027991081 scopus 로고
    • Estimation of changes in side chain configurational entropy in binding and folding: General methods and application to helix formation
    • Lee KH, Xie D, Freire E, Amzel LM. 1994. Estimation of changes in side chain configurational entropy in binding and folding: General methods and application to helix formation. Proteins 20:68-84.
    • (1994) Proteins , vol.20 , pp. 68-84
    • Lee, K.H.1    Xie, D.2    Freire, E.3    Amzel, L.M.4
  • 17
    • 0031564662 scopus 로고    scopus 로고
    • Estimating the relative populations of 3(10)-helix and alpha-helix in Ala-rich peptides: A hydrogen exchange and high field NMR study
    • Millhauser GL, Stenland CJ, Hanson P, Bolin KA, van de Ven FJ. 1997. Estimating the relative populations of 3(10)-helix and alpha-helix in Ala-rich peptides: A hydrogen exchange and high field NMR study. J Mol Biol 267:963-974.
    • (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.5
  • 18
    • 0028568650 scopus 로고
    • Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: Comparison with experimental scales
    • Muñoz V, Serrano L. 1994. Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices: Comparison with experimental scales. Proteins 20:301-311.
    • (1994) Proteins , vol.20 , pp. 301-311
    • Muñoz, V.1    Serrano, L.2
  • 19
    • 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, Serrano L. 1995a. 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 245:275-296.
    • (1995) J Mol Biol , vol.245 , pp. 275-296
    • Muñoz, V.1    Serrano, L.2
  • 20
    • 0029155035 scopus 로고
    • Helix design, prediction and stability
    • Muñoz V, Serrano L. 1995b. Helix design, prediction and stability. Curr Opin Biotechnol 6:382-386.
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 382-386
    • Muñoz, V.1    Serrano, L.2
  • 21
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • Muñoz V, Serrano L. 1997. Development of the multiple sequence approximation within the AGADIR model of alpha-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
  • 22
    • 0023338543 scopus 로고
    • Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides
    • Ooi T, Oobatake M, Nemethy G, Scheraga HA. 1987. Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides. Proc Natl Acad Sci USA 84:3086-3090.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3086-3090
    • Ooi, T.1    Oobatake, M.2    Nemethy, G.3    Scheraga, H.A.4
  • 23
    • 0033582944 scopus 로고    scopus 로고
    • Side-chain structures in the first turn of the alpha-helix
    • Penel S, Hughes E, Doig AJ. 1999. Side-chain structures in the first turn of the alpha-helix. J Mol Biol 287:127-143.
    • (1999) J Mol Biol , vol.287 , pp. 127-143
    • Penel, S.1    Hughes, E.2    Doig, A.J.3
  • 24
    • 0032562654 scopus 로고    scopus 로고
    • Position dependence of non-polar amino acid intrinsic helical propensities
    • Petukhov M, Muñoz V, Yumoto N, Yoshikawa S, Serrano L. 1998. Position dependence of non-polar amino acid intrinsic helical propensities. J Mol Biol 278:279-289.
    • (1998) J Mol Biol , vol.278 , pp. 279-289
    • Petukhov, M.1    Muñoz, V.2    Yumoto, N.3    Yoshikawa, S.4    Serrano, L.5
  • 25
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of alpha helices
    • Richardson JS, Richardson DC. 1988. Amino acid preferences for specific locations at the ends of alpha helices. Science 240:1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 26
    • 0030447864 scopus 로고    scopus 로고
    • Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol
    • Rohl CA, Chakrabartty A, Baldwin RL. 1996. Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol. Protein Sci 5:2623-2637.
    • (1996) Protein Sci , vol.5 , pp. 2623-2637
    • Rohl, C.A.1    Chakrabartty, A.2    Baldwin, R.L.3
  • 27
    • 0029147823 scopus 로고
    • Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structures
    • Swindells MB, MacArthur MW, Thornton JM. 1995. Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structures. Nature Struct Biol 2:596-603.
    • (1995) Nature Struct Biol , vol.2 , pp. 596-603
    • Swindells, M.B.1    MacArthur, M.W.2    Thornton, J.M.3
  • 28
    • 0025398721 scopus 로고
    • What If: A molecular modeling and drug design program
    • Vriend G. 1990. WHAT IF: A molecular modeling and drug design program. J Mol Graph 8:52-56.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 29
    • 0027080909 scopus 로고
    • Atomic solvation parameters applied to molecular dynamics of proteins in solution
    • Wesson L, Eisenberg D. 1992. Atomic solvation parameters applied to molecular dynamics of proteins in solution. Protein Sci 1:227-235.
    • (1992) Protein Sci , vol.1 , pp. 227-235
    • Wesson, L.1    Eisenberg, D.2
  • 30
    • 0017435119 scopus 로고
    • Conformational analysis of the 20 naturally occurring amino acid residues using ECEPP
    • Zimmerman SS, Pottle MS, Nemethy G, Scheraga HA. 1977. Conformational analysis of the 20 naturally occurring amino acid residues using ECEPP. Macromolecules 10:1-9.
    • (1977) Macromolecules , vol.10 , pp. 1-9
    • Zimmerman, S.S.1    Pottle, M.S.2    Nemethy, G.3    Scheraga, H.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.