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Volumn 36, Issue 1, 2002, Pages 1-18

Temperature-induced formation of a non-native intermediate state of the all β-sheet protein CD2

Author keywords

Domain swapping; Folding of sheet proteins; Non native intermediate; Quantitative protein secondary structural analysis; Thermal denaturation

Indexed keywords

1-ANILINO-8-NAPHTHALENESULFONATE; 8 ANILINO 1 NAPHTHALENESULFONIC ACID; CD2 1 CELL ADHESION PROTEIN, RAT; CD2 ANTIGEN; CD2-1 CELL ADHESION PROTEIN, RAT; FLUORESCENT DYE;

EID: 0036358461     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/cbb:36:1:01     Document Type: Article
Times cited : (10)

References (90)
  • 1
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal, C. (1968) Are there pathways for protein folding? J. Chim. Phys. 65, 44-45.
    • (1968) J. Chim. Phys. , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 2
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K. A. and Chan, H. S. (1997) From Levinthal to pathways to funnels. Nat. Struct. Biol. 4, 10-19.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 4
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. (1989) The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6, 87-103.
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 5
    • 0001889857 scopus 로고
    • Characterizing intermediates in protein folding
    • Creighton, T. E. (1991) Characterizing intermediates in protein folding. Curr. Biol. 1, 8-10.
    • (1991) Curr. Biol. , vol.1 , pp. 8-10
    • Creighton, T.E.1
  • 6
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford, S. E., Dobson, C. M., and Evans, P. A. (1992) The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 358, 302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 8
    • 0029160445 scopus 로고
    • How the molten globule became
    • Ptitsyn, O. B. (1995) How the molten globule became. Trends Biochem. Sci. 20, 376-379.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 376-379
    • Ptitsyn, O.B.1
  • 9
    • 0029569051 scopus 로고
    • Protein Fold recognition
    • Shortle, D. (1995) Protein Fold recognition. Nat. Struct. Biol. 2, 91-93.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 91-93
    • Shortle, D.1
  • 11
    • 0024533979 scopus 로고
    • Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guineapig alpha-lactalbumin
    • Baum, J., Dobson, C. M., Evans, P. A., and Hanley, C. (1989) Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guineapig alpha-lactalbumin. Biochemistry 28, 7-13.
    • (1989) Biochemistry , vol.28 , pp. 7-13
    • Baum, J.1    Dobson, C.M.2    Evans, P.A.3    Hanley, C.4
  • 12
    • 0027280472 scopus 로고
    • Structure and stability of the molten globule state of guineapig alpha-lactalbumin: A hydrogen exchange study
    • Chyan, C.-L., Wormald, C., Dobson, C. M., Evans, P. A., and Baum, J. (1993) Structure and stability of the molten globule state of guineapig alpha-lactalbumin: a hydrogen exchange study. Biochemistry 32, 5681-5691.
    • (1993) Biochemistry , vol.32 , pp. 5681-5691
    • Chyan, C.-L.1    Wormald, C.2    Dobson, C.M.3    Evans, P.A.4    Baum, J.5
  • 13
    • 0027749370 scopus 로고
    • Formation of a molten globute intermediate early in the kinetic folding pathway of apomyglobin
    • Jennings, P. A. and Wright, P. E. (1993) Formation of a molten globute intermediate early in the kinetic folding pathway of apomyglobin. Science 262, 892-895.
    • (1993) Science , vol.262 , pp. 892-895
    • Jennings, P.A.1    Wright, P.E.2
  • 15
    • 0021114569 scopus 로고
    • 'Molten globule state': A compact form of globular proteins with mobile side-chains
    • Ohgushi, M. and Wada, A. (1983) 'Molten globule state': a compact form of globular proteins with mobile side-chains. FEBS Lett. 164, 21-24.
    • (1983) FEBS Lett. , vol.164 , pp. 21-24
    • Ohgushi, M.1    Wada, A.2
  • 17
    • 0029040449 scopus 로고
    • Thermodynamic stability of the molten globule states of apomyoglobin
    • Nishii, I., Kataoka, M., and Goto, Y. (1995) Thermodynamic stability of the molten globule states of apomyoglobin. J. Mol. Biol. 250, 223-238.
    • (1995) J. Mol. Biol. , vol.250 , pp. 223-238
    • Nishii, I.1    Kataoka, M.2    Goto, Y.3
  • 18
    • 0030010408 scopus 로고    scopus 로고
    • Intermediate states in protein folding
    • Privalov, P. L. (1996) Intermediate states in protein folding. J. Mol. Biol. 258, 707-725.
    • (1996) J. Mol. Biol. , vol.258 , pp. 707-725
    • Privalov, P.L.1
  • 19
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2.1. Evidence for a two-state transition
    • Jackson, S. E. and Fersht, A. R. (1991) Folding of chymotrypsin inhibitor 2.1. Evidence for a two-state transition. Biochemistry 30, 10,428-10,435.
    • (1991) Biochemistry , vol.30
    • Jackson, S.E.1    Fersht, A.R.2
  • 20
    • 0028331876 scopus 로고
    • Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition
    • Viguera, A. R., Martínez, J. C., Filimonov, V. V., Mateo, P. L., and Serrano, L. (1994) Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition. Biochemistry 33, 2142-2150.
    • (1994) Biochemistry , vol.33 , pp. 2142-2150
    • Viguera, A.R.1    Martínez, J.C.2    Filimonov, V.V.3    Mateo, P.L.4    Serrano, L.5
  • 21
    • 0027364930 scopus 로고
    • Dissecting the structure of a partially folded protein. Circular dichroism and nuclear magnetic resonance studies of peptides from ubiquitin
    • Cox, J. P. L., Evans, P. A., Packman, L. C., Williams, D. H., and Woolfson, D. N. (1993) Dissecting the structure of a partially folded protein. Circular dichroism and nuclear magnetic resonance studies of peptides from ubiquitin. J. Mol. Biol. 234, 483-492.
    • (1993) J. Mol. Biol. , vol.234 , pp. 483-492
    • Cox, J.P.L.1    Evans, P.A.2    Packman, L.C.3    Williams, D.H.4    Woolfson, D.N.5
  • 22
    • 0027305989 scopus 로고
    • Folding and stability of a tryptophan-containing mutant of ubiquitin
    • Khorasanizadeh, S., Peters, I. D., Butt, T. R., and Roder, H. (1993) Folding and stability of a tryptophan-containing mutant of ubiquitin. Biochemistry 32, 7054-7063.
    • (1993) Biochemistry , vol.32 , pp. 7054-7063
    • Khorasanizadeh, S.1    Peters, I.D.2    Butt, T.R.3    Roder, H.4
  • 23
    • 0030716169 scopus 로고    scopus 로고
    • Cavity formation before stable hydrogen bonding in the folding of a beta-clam protein
    • Clark, P. L., Liu, Z. P., Rizo, J., and Gierasch, L. M. (1997) Cavity formation before stable hydrogen bonding in the folding of a beta-clam protein. Nat. Struct. Biol. 4, 883-886.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 883-886
    • Clark, P.L.1    Liu, Z.P.2    Rizo, J.3    Gierasch, L.M.4
  • 24
    • 0028176595 scopus 로고
    • Context is a major determinant of beta-sheet propensity
    • Minor, D. L., Jr. and Kim, P. S. (1994) Context is a major determinant of beta-sheet propensity. Nature 367, 660-663.
    • (1994) Nature , vol.367 , pp. 660-663
    • Minor Jr., D.L.1    Kim, P.S.2
  • 25
    • 0028467159 scopus 로고
    • Protein structure. Born to be beta
    • Regan, L. (1994) Protein structure. Born to be beta. Curr. Biol. 7, 656-658.
    • (1994) Curr. Biol. , vol.7 , pp. 656-658
    • Regan, L.1
  • 27
    • 0029092697 scopus 로고
    • Conformational properties of four peptides spanning the sequence of hen lysozyme
    • Yang, J. J., Buck, M., Pitkeathly M., Kotik, M., Haynie, D. T., Dobson, C. M., et al. (1995) Conformational properties of four peptides spanning the sequence of hen lysozyme. J. Mol. Biol. 252, 483-491.
    • (1995) J. Mol. Biol. , vol.252 , pp. 483-491
    • Yang, J.J.1    Buck, M.2    Pitkeathly, M.3    Kotik, M.4    Haynie, D.T.5    Dobson, C.M.6
  • 28
    • 0032007299 scopus 로고    scopus 로고
    • Kinetic studies of beta-sheet protein folding
    • Capaldi, A. P. and Radford, S. E. (1998) Kinetic studies of beta-sheet protein folding. Curr. Opin. Struct. Biol. 8, 86-92.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 86-92
    • Capaldi, A.P.1    Radford, S.E.2
  • 29
    • 0031594158 scopus 로고    scopus 로고
    • A folding pathway for betapep-4 peptide 33 mer: From unfolded monomers and beta-sheet sandwich dimers to well-structured tetramers
    • Mayo, K. H. and Ilyina, E. (1998) A folding pathway for betapep-4 peptide 33 mer: from unfolded monomers and beta-sheet sandwich dimers to well-structured tetramers. Protein Sci. 7, 358-368.
    • (1998) Protein Sci. , vol.7 , pp. 358-368
    • Mayo, K.H.1    Ilyina, E.2
  • 30
    • 0031010678 scopus 로고    scopus 로고
    • Amide backbone and water-related H/D isotope effects on the dynamics of a protein folding reaction
    • Parker, M. J. and Clarke, A. R. (1997) Amide backbone and water-related H/D isotope effects on the dynamics of a protein folding reaction. Biochemistry 36, 5786-5794.
    • (1997) Biochemistry , vol.36 , pp. 5786-5794
    • Parker, M.J.1    Clarke, A.R.2
  • 31
    • 0030871209 scopus 로고    scopus 로고
    • Acquisition of native beta-strand topology during the rapid collapse phase of protein folding
    • Parker, M. J., Dempsey, C. E., Lorch, M., and Clarke, A. R. (1997) Acquisition of native beta-strand topology during the rapid collapse phase of protein folding. Biochemistry 36, 13,396-13,405.
    • (1997) Biochemistry , vol.36
    • Parker, M.J.1    Dempsey, C.E.2    Lorch, M.3    Clarke, A.R.4
  • 32
    • 0031892524 scopus 로고    scopus 로고
    • Topology, sequence evolution and folding dynamics of an immunoglobulin domain
    • Parker, M. J., Dempsey, C. E., Hosszu, L. L., Waltho, J. P., and Clarke, A. R. (1998) Topology, sequence evolution and folding dynamics of an immunoglobulin domain. Nat. Struct. Biol. 5, 194-198.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 194-198
    • Parker, M.J.1    Dempsey, C.E.2    Hosszu, L.L.3    Waltho, J.P.4    Clarke, A.R.5
  • 33
    • 0032562178 scopus 로고    scopus 로고
    • Thermodynamic properties of transient intermediates and transition states in the folding of two contrasting protein structures
    • Parker, M. J., Lorch, M., Sessions, R. B., and Clarke, A. R. (1998) Thermodynamic properties of transient intermediates and transition states in the folding of two contrasting protein structures. Biochemistry 37, 2538-2545.
    • (1998) Biochemistry , vol.37 , pp. 2538-2545
    • Parker, M.J.1    Lorch, M.2    Sessions, R.B.3    Clarke, A.R.4
  • 34
    • 0026059140 scopus 로고
    • Structure of domain 1 of rat T lymphocyle CD2 antigen
    • Driscoll, P. C., Cyster, J. G., Campbell, I. D., and Williams, A. F. (1991) Structure of domain 1 of rat T lymphocyle CD2 antigen. Nature 353, 762-765.
    • (1991) Nature , vol.353 , pp. 762-765
    • Driscoll, P.C.1    Cyster, J.G.2    Campbell, I.D.3    Williams, A.F.4
  • 35
    • 0026488252 scopus 로고
    • Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2
    • Jones, E. Y., Davis, S. J., Williams, A. F., Harlos, K., and Stuart, D. I. (1992) Crystal structure at 2.8 Å resolution of a soluble form of the cell adhesion molecule CD2. Nature 360, 232-239.
    • (1992) Nature , vol.360 , pp. 232-239
    • Jones, E.Y.1    Davis, S.J.2    Williams, A.F.3    Harlos, K.4    Stuart, D.I.5
  • 36
    • 0029133626 scopus 로고
    • Conformation and function of the N-linked glycan in the adhesion domain of human CD2
    • Wyss, D. F., Choi, J. S., Li, J., Knoppers, M. H., Willis, K. J., Arulanandam, A. R., et al. (1995) Conformation and function of the N-linked glycan in the adhesion domain of human CD2. Science, 269, 1273-1278.
    • (1995) Science , vol.269 , pp. 1273-1278
    • Wyss, D.F.1    Choi, J.S.2    Li, J.3    Knoppers, M.H.4    Willis, K.J.5    Arulanandam, A.R.6
  • 38
    • 0031662892 scopus 로고    scopus 로고
    • Engineering an intertwined form of CD2 for stability and assembly
    • Murray, A. J., Head, J. G., Barker, J. J., and Brady, R. L. (1998) Engineering an intertwined form of CD2 for stability and assembly. Nat. Struct. Biol. 5, 778-782.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 778-782
    • Murray, A.J.1    Head, J.G.2    Barker, J.J.3    Brady, R.L.4
  • 39
    • 0029117494 scopus 로고
    • Finding the right fold
    • Dobson, C. M. (1995) Finding the right fold. Struct. Biol. 2, 513-517.
    • (1995) Struct. Biol. , vol.2 , pp. 513-517
    • Dobson, C.M.1
  • 41
    • 0002439879 scopus 로고
    • Circular dichroism of peptides
    • Woody, R. W. (1985) Circular dichroism of peptides. Peptides 7, 15-114.
    • (1985) Peptides , vol.7 , pp. 15-114
    • Woody, R.W.1
  • 42
    • 0027917894 scopus 로고
    • Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2
    • Withka, J. M., Wyss, D. F., Wagner, G., Arulanandam, A. R., Reinherz, E. L., and Recny, M. A. (1993) Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2. Structure 1, 69-81.
    • (1993) Structure , vol.1 , pp. 69-81
    • Withka, J.M.1    Wyss, D.F.2    Wagner, G.3    Arulanandam, A.R.4    Reinherz, E.L.5    Recny, M.A.6
  • 44
    • 0033548458 scopus 로고    scopus 로고
    • The Greek key protein apo-pseudoazurin folds through an obligate on- Pathway intermediate
    • Capaldi, A. P., Ferguson, S. J., and Radford, S. E. (1999) The Greek key protein apo-pseudoazurin folds through an obligate on- pathway intermediate. J. Mol. Biol. 286, 1621-1632.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1621-1632
    • Capaldi, A.P.1    Ferguson, S.J.2    Radford, S.E.3
  • 45
    • 0026411154 scopus 로고
    • Copper protein structures
    • Adman, E. T. (1991) Copper protein structures. Adv. Protein Chem. 42, 145-197.
    • (1991) Adv. Protein Chem. , vol.42 , pp. 145-197
    • Adman, E.T.1
  • 46
    • 0032080047 scopus 로고    scopus 로고
    • Structural determinants in the sequences of immunoglobulin variable domain
    • Chothia, C., Gelfand, I., and Kister, A. (1998) Structural determinants in the sequences of immunoglobulin variable domain. J. Mol. Biol. 278, 457-479.
    • (1998) J. Mol. Biol. , vol.278 , pp. 457-479
    • Chothia, C.1    Gelfand, I.2    Kister, A.3
  • 47
    • 0026628269 scopus 로고
    • Deconvolution of the circular dichroism spectra of protein: The circular dichroism spectra of the antiparallel β-sheet in proteins
    • Perczel, A., Park, K., and Fasman, G. D. (1992) Deconvolution of the circular dichroism spectra of protein: the circular dichroism spectra of the antiparallel β-sheet in proteins. Proteins 13, 57-69.
    • (1992) Proteins , vol.13 , pp. 57-69
    • Perczel, A.1    Park, K.2    Fasman, G.D.3
  • 48
    • 0027527209 scopus 로고
    • Circular dichroism studies of barnase and its mutants: Characterization of the contribution of aromatic side chains
    • Vuilleumier, S., Sancho, J., Loewenthal, R., and Fersht, A. R. (1993) Circular dichroism studies of barnase and its mutants: characterization of the contribution of aromatic side chains. Biochemistry 32, 10,303-10,313.
    • (1993) Biochemistry , vol.32
    • Vuilleumier, S.1    Sancho, J.2    Loewenthal, R.3    Fersht, A.R.4
  • 49
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov, P. L. and Khechinashvili, N. N. (1974) A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J. Mol. Biol. 86, 665-684.
    • (1974) J. Mol. Biol. , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 50
    • 0028132243 scopus 로고
    • Thermal unfolding of tetrametic melittin: Comparison with the molten globule state of cytochrome c
    • Hagihara, Y., Oobayake, M., and Goto, Y. (1994) Thermal unfolding of tetrametic melittin: Comparison with the molten globule state of cytochrome c. Protein Sci. 3, 1418-1429.
    • (1994) Protein Sci. , vol.3 , pp. 1418-1429
    • Hagihara, Y.1    Oobayake, M.2    Goto, Y.3
  • 51
    • 0027980588 scopus 로고
    • Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: Evidence for residual electrostatic interactions in the acid/thermally denatured state
    • Oliveberg, M., Vuilleumier, S., and Fersht, A. R. (1994) Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: evidence for residual electrostatic interactions in the acid/thermally denatured state. Biochemistry 33, 8826-8832.
    • (1994) Biochemistry , vol.33 , pp. 8826-8832
    • Oliveberg, M.1    Vuilleumier, S.2    Fersht, A.R.3
  • 52
    • 0029864592 scopus 로고    scopus 로고
    • Thermal unfolding of human high-density apolipoprotein A-1: Implications for a lipid-free molten globular state
    • Gursky, O. and Atkinson, D. (1996) Thermal unfolding of human high-density apolipoprotein A-1: implications for a lipid-free molten globular state. Proc. Natl. Acad. Sci. USA 93, 2991-2995.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2991-2995
    • Gursky, O.1    Atkinson, D.2
  • 53
    • 0343580520 scopus 로고    scopus 로고
    • Circular dichroism of denatured barstar suggests residual structure
    • Nolting, B., Golbik, R., Soler-Gonzalez, A. S., and Fersht, A. R. (1997) Circular dichroism of denatured barstar suggests residual structure. Biochemistry 36, 9899-9905.
    • (1997) Biochemistry , vol.36 , pp. 9899-9905
    • Nolting, B.1    Golbik, R.2    Soler-Gonzalez, A.S.3    Fersht, A.R.4
  • 54
    • 0028102759 scopus 로고
    • Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins
    • Woody, R. W. (1994) Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins. Eur. Biophys. J. 23, 253-262.
    • (1994) Eur. Biophys. J. , vol.23 , pp. 253-262
    • Woody, R.W.1
  • 56
    • 0033578401 scopus 로고    scopus 로고
    • Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: Circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor
    • Sreerama, N., Manning, M. C., Powers, M. E., Zhang, J. X., Goldenberg, D. P., and Woody, R. W. (1999) Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor. Biochemistry 38, 10,814-10,822.
    • (1999) Biochemistry , vol.38
    • Sreerama, N.1    Manning, M.C.2    Powers, M.E.3    Zhang, J.X.4    Goldenberg, D.P.5    Woody, R.W.6
  • 57
    • 0026608073 scopus 로고
    • Environment affects amino acid preference for secondary structure
    • Zhong, L. and Johnson, W. C., Jr. (1992) Environment affects amino acid preference for secondary structure. Pro. Nat. Acad. Sci. USA 89, 4462-4465.
    • (1992) Pro. Nat. Acad. Sci. USA , vol.89 , pp. 4462-4465
    • Zhong, L.1    Johnson Jr., W.C.2
  • 58
    • 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, 5560-5565.
    • (1993) Biochemistry , vol.32 , pp. 5560-5565
    • Chakrabartty, A.1    Kortemme, T.2    Padmanabhan, S.3    Baldwin, R.L.4
  • 59
    • 0028343072 scopus 로고
    • Far-UV circular dichroism reveals a conformational switch in a peptide fragment from the beta-sheet of hen lysozyme
    • Yang, J. J., Pikeathly, M., and Radford, S. E. (1994) Far-UV circular dichroism reveals a conformational switch in a peptide fragment from the beta-sheet of hen lysozyme. Biochemistry 33, 7345-7353.
    • (1994) Biochemistry , vol.33 , pp. 7345-7353
    • Yang, J.J.1    Pikeathly, M.2    Radford, S.E.3
  • 60
    • 0022463740 scopus 로고
    • Resolution-enhanced fourier transform infrared spectroscopy of enzymes
    • Susi, H. and Byler, D. M. (1986) Resolution-enhanced fourier transform infrared spectroscopy of enzymes. Methods Enzymol. 130, 290-311.
    • (1986) Methods Enzymol. , vol.130 , pp. 290-311
    • Susi, H.1    Byler, D.M.2
  • 61
    • 0024291269 scopus 로고
    • Fourier transform infrared spectra of the polypeptide alamethicin and a possible structural similarity with bacteriorhodopsin
    • Haris, P. I. and Chapman, D. (1988) Fourier transform infrared spectra of the polypeptide alamethicin and a possible structural similarity with bacteriorhodopsin. Biochim. Biophys. Acta. 943, 375-380.
    • (1988) Biochim. Biophys. Acta. , vol.943 , pp. 375-380
    • Haris, P.I.1    Chapman, D.2
  • 62
    • 0000316288 scopus 로고
    • Fourier transform infrared spectroscopic studies of lipids, polypeptides and proteins
    • Jackson, M., Haris, P. I., and Chapman, D. (1989) Fourier transform infrared spectroscopic studies of lipids, polypeptides and proteins. J. Mol. Struct. 214, 329-355.
    • (1989) J. Mol. Struct. , vol.214 , pp. 329-355
    • Jackson, M.1    Haris, P.I.2    Chapman, D.3
  • 63
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by fourier transform infrared spectroscopy: A critical assessment
    • Surewicz, W. K., Mantsch, H. H., and Chapman, D. (1993) Determination of protein secondary structure by fourier transform infrared spectroscopy: a critical assessment. Biochemistry 32, 389-394.
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 64
    • 0029863555 scopus 로고    scopus 로고
    • A novel function for the second C2 domain of synaptotagmin
    • Chapman, E. R., An, S., Edwardson, J. M., and Jahn, R. (1996) A novel function for the second C2 domain of synaptotagmin. J. Biol. Chem. 271, 5844-5849.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5844-5849
    • Chapman, E.R.1    An, S.2    Edwardson, J.M.3    Jahn, R.4
  • 65
    • 0000882508 scopus 로고    scopus 로고
    • An FTIR study of the complex melting behaviour of alpha-lactalbumin
    • Zhong, H., Gilmanshin, R., and Callender, R. (1999) An FTIR study of the complex melting behaviour of alpha-lactalbumin. J. Phys. Chem 103, 39,947-39,953.
    • (1999) J. Phys. Chem , vol.103
    • Zhong, H.1    Gilmanshin, R.2    Callender, R.3
  • 66
    • 0342679998 scopus 로고    scopus 로고
    • Transient non-native secondary structures during the refolding of alpha- Lactalbumin detected by infrared spectroscopy
    • Troullier, A., Reinstadler, D., Dupont, Y., Naumann, D., and Forge, V. (2000) Transient non-native secondary structures during the refolding of alpha- lactalbumin detected by infrared spectroscopy. Nat. Struct. Biol. 7, 78-86.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 78-86
    • Troullier, A.1    Reinstadler, D.2    Dupont, Y.3    Naumann, D.4    Forge, V.5
  • 67
    • 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, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 68
    • 0023442501 scopus 로고
    • Fourier transform infrared study of proteins with parallel beta-chains
    • Susi, H. and Byler, D. M. (1987) Fourier transform infrared study of proteins with parallel beta-chains. Arch. Biochem. Biophys. 258, 465-469.
    • (1987) Arch. Biochem. Biophys. , vol.258 , pp. 465-469
    • Susi, H.1    Byler, D.M.2
  • 70
    • 0016797947 scopus 로고
    • Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water
    • Chirgadze, Y. N., Fedorov, O. V., and Trushina, N. P. (1975) Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water. Biopolymers 14, 679-694.
    • (1975) Biopolymers , vol.14 , pp. 679-694
    • Chirgadze, Y.N.1    Fedorov, O.V.2    Trushina, N.P.3
  • 71
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro, M. M. and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 72
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4, 2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 73
    • 0032570265 scopus 로고    scopus 로고
    • Structure and stability of the N-terminal domain of the ribosomal protein L9: Evidence for rapid two-state folding
    • Kuhlman, B., Boice, J. A., Fairman, R., and Raleigh, D. P. (1998) Structure and stability of the N-terminal domain of the ribosomal protein L9: evidence for rapid two-state folding. Biochemistry 37, 1025-1032.
    • (1998) Biochemistry , vol.37 , pp. 1025-1032
    • Kuhlman, B.1    Boice, J.A.2    Fairman, R.3    Raleigh, D.P.4
  • 75
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford, C. (1968) Protein denaturation. Adv. Protein Chem. 23, 121-282.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 76
    • 0030001915 scopus 로고    scopus 로고
    • On the entropy of protein folding
    • Makhatadze, G. I. and Privalov, P. L. (1996) On the entropy of protein folding. Protein Sci. 5, 507-510.
    • (1996) Protein Sci. , vol.5 , pp. 507-510
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 77
    • 0028009149 scopus 로고
    • SOPM: A self-optimized method for protein secondary structure prediction
    • Geourjon, C. and Deleage, G. (1994) SOPM: a self-optimized method for protein secondary structure prediction. Protein Eng. 7, 157-164.
    • (1994) Protein Eng. , vol.7 , pp. 157-164
    • Geourjon, C.1    Deleage, G.2
  • 78
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from amino acid sequence
    • Garnier, J., Gibrat, J. F., and Robson, B. (1996) GOR method for predicting protein secondary structure from amino acid sequence. Methods Enzymol. 266, 540-553.
    • (1996) Methods Enzymol. , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.F.2    Robson, B.3
  • 79
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B. and Sander, C. (1993) Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 80
    • 0028172534 scopus 로고
    • The Immunoglobulin fold structural classification, sequence patterns and common core
    • Bork, P., Holm, L., and Sander, C. (1994) The Immunoglobulin fold structural classification, sequence patterns and common core. J. Mol. Biol. 242, 309-320.
    • (1994) J. Mol. Biol. , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 81
    • 0029588554 scopus 로고
    • High helical propensity of the peptide fragments derived from beta- Lactoglobulin, a predominantly beta-sheet protein
    • Hamada, D., Kuroda, Y., Tanaka, T., and Goto, Y. (1995) High helical propensity of the peptide fragments derived from beta- lactoglobulin, a predominantly beta-sheet protein. J. Mol. Biol. 254, 737-746.
    • (1995) J. Mol. Biol. , vol.254 , pp. 737-746
    • Hamada, D.1    Kuroda, Y.2    Tanaka, T.3    Goto, Y.4
  • 82
    • 0028978422 scopus 로고
    • Trifluoroethanol-induced stabilization of a-helical structure of β-lactoglobulin: Implication for non-hierarchical protein folding
    • Shiraki, K., Nishikawa, K., and Goto, Y. (1995) Trifluoroethanol-induced stabilization of a-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245, 180-194.
    • (1995) J. Mol. Biol. , vol.245 , pp. 180-194
    • Shiraki, K.1    Nishikawa, K.2    Goto, Y.3
  • 83
    • 0029738546 scopus 로고    scopus 로고
    • Induction of alpha-helix in the beta-sheet protein tumor necrosis factor-alpha: Acid-induced denaturation
    • Narhi, L. O., Philo, J. S., Li, T., Zhang, M., Samal, B., and Arakawa, T. (1996) Induction of alpha-helix in the beta-sheet protein tumor necrosis factor-alpha: acid-induced denaturation. Biochemistry 35, 11,454-11,460.
    • (1996) Biochemistry , vol.35
    • Narhi, L.O.1    Philo, J.S.2    Li, T.3    Zhang, M.4    Samal, B.5    Arakawa, T.6
  • 84
    • 0029781028 scopus 로고    scopus 로고
    • Induction of alpha-helix in the beta-sheet protein tumor necrosis factor-alpha: Thermal- and trifluoroethanol-induced denaturation at neutral pH
    • Narhi, L. O., Philo, J. S., Li, T., Zhang, M., Samal, B., and Arakawa, T. (1996) Induction of alpha-helix in the beta-sheet protein tumor necrosis factor-alpha: thermal- and trifluoroethanol-induced denaturation at neutral pH. Biochemistry 35, 11,447-11,453.
    • (1996) Biochemistry , vol.35
    • Narhi, L.O.1    Philo, J.S.2    Li, T.3    Zhang, M.4    Samal, B.5    Arakawa, T.6
  • 85
    • 0029740071 scopus 로고    scopus 로고
    • Non-native alpha-helical intermediate in the refolding of beta- Lactoglobulin, a predominantly beta-sheet protein
    • Hamada, D., Segawa, S., and Goto, Y. (1996) Non-native alpha-helical intermediate in the refolding of beta- lactoglobulin, a predominantly beta-sheet protein. Nat. Struct. Biol. 3, 868-873.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 868-873
    • Hamada, D.1    Segawa, S.2    Goto, Y.3
  • 86
    • 0030726361 scopus 로고    scopus 로고
    • pH and temperature-induced molten globule-like denatured states of equinatoxin II: A study by UV-melting, DSC, far-and near-UV CD spectroscopy, and ANS fluorescence
    • Poklar, N., Lah, J., Salobir, M., Macek, P., and Vesnaver, G. (1997) pH and temperature-induced molten globule-like denatured states of equinatoxin II: a study by UV-melting, DSC, far-and near-UV CD spectroscopy, and ANS fluorescence. Biochemistry 36, 14,345-14,352.
    • (1997) Biochemistry , vol.36
    • Poklar, N.1    Lah, J.2    Salobir, M.3    Macek, P.4    Vesnaver, G.5
  • 87
    • 0031580203 scopus 로고    scopus 로고
    • The equilibrium intermediate of beta-lactoglobulin with non-native alpha-helical structure
    • Hamada, D. and Goto, Y. (1997) The equilibrium intermediate of beta-lactoglobulin with non-native alpha-helical structure J. Mol. Biol. 269, 479-487.
    • (1997) J. Mol. Biol. , vol.269 , pp. 479-487
    • Hamada, D.1    Goto, Y.2
  • 88
    • 0027440139 scopus 로고
    • Acid-induced unfolding of brain-derived neurotrophic factor results in the formation of a monomeric 'A state'
    • Narhi, L. O., Rosenfeld, R., Wen, J., Arakawa, T., Prestrelski, S. J., and Philo, J. S. (1993) Acid-induced unfolding of brain-derived neurotrophic factor results in the formation of a monomeric 'A state'. Biochemistry 32, 10,819-10,825.
    • (1993) Biochemistry , vol.32
    • Narhi, L.O.1    Rosenfeld, R.2    Wen, J.3    Arakawa, T.4    Prestrelski, S.J.5    Philo, J.S.6
  • 89
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett, M. J., Schlunegger, M. P., and Eisenberg, D. (1995) 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4, 2455-2468.
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 90
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger, M. P., Bennett, M. J., and Eisenberg, D. (1997) Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly Adv. Protein Chem. 50, 61-122.
    • (1997) Adv. Protein Chem. , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3


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