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Volumn 252, Issue 3, 1995, Pages 351-365

Free Energy Determinants of Secondary Structure Formation: I. Α-Helices

Author keywords

Conformational entropy; Helix coil transition; Hydrogen bonding; Protein stability; helix propensity

Indexed keywords

ALANINE; GLYCINE;

EID: 0029121068     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1995.0502     Document Type: Article
Times cited : (228)

References (66)
  • 1
    • 0023675175 scopus 로고
    • Microfolding: Conformational probability map for the alanine dipeptide in water from molecular dynamics simulations
    • Anderson, A. G. & Hermans, J. (1988). Microfolding: conformational probability map for the alanine dipeptide in water from molecular dynamics simulations. Proteins: Struct. Funct. Genet. 3, 262-264.
    • (1988) Proteins: Struct. Funct. Genet. , vol.3 , pp. 262-264
    • Anderson, A.G.1    Hermans, J.2
  • 3
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic effect in protein folding
    • Baldwin, R. (1986). Temperature dependence of the hydrophobic effect in protein folding. Proc. Natl Acad. Sci. USA, 83, 8069-8072.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 8069-8072
    • Baldwin, R.1
  • 4
    • 0020119906 scopus 로고
    • A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A
    • Bierzynsky A., Kim, P. S. & Baldwin, R. L. (1982). A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A. Proc. Natl Acad. Sci. USA, 79, 2470-2474.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 2470-2474
    • Bierzynsky, A.1    Kim, P.S.2    Baldwin, R.L.3
  • 5
    • 84984085214 scopus 로고
    • Effect of hydrophobic bonding on the stability of poly-L-ala-nine helices in water
    • Bixon, M., Scheraga, H. A. & Lifson, S. (1963). Effect of hydrophobic bonding on the stability of poly-L-ala-nine helices in water. Biopolymers, 1, 419-429.
    • (1963) Biopolymers , vol.1 , pp. 419-429
    • Bixon, M.1    Scheraga, H.A.2    Lifson, S.3
  • 7
    • 0041140017 scopus 로고
    • Simulations of peptide conformational dynamics and thermodynamics
    • Brooks, C. L. & Case, D. A. (1993). Simulations of peptide conformational dynamics and thermodynamics. Chem. Rev. 93, 2487-2502.
    • (1993) Chem. Rev. , vol.93 , pp. 2487-2502
    • Brooks, C.L.1    Case, D.A.2
  • 9
    • 0028222235 scopus 로고
    • Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions
    • Chakrabartty A., Kortemme, T. & Baldwin, R. L. (1994). Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Protein Sci. 3, 843-852.
    • (1994) Protein Sci , vol.3 , pp. 843-852
    • Chakrabartty, A.1    Kortemme, T.2    Baldwin, R.L.3
  • 10
    • 2342541375 scopus 로고
    • Solvation: Effects of molecular size and shape
    • Chan, H. S. & Dill, K. A. (1994). Solvation: effects of molecular size and shape. J. Chem. Phys. 101, 7007-7026.
    • (1994) J. Chem. Phys. , vol.101 , pp. 7007-7026
    • Chan, H.S.1    Dill, K.A.2
  • 11
    • 0017187836 scopus 로고
    • The nature of the accessible and buried surface in proteins
    • Chothia, C. (1976). The nature of the accessible and buried surface in proteins. J. Mol. Biol. 105, 1-14.
    • (1976) J. Mol. Biol. , vol.105 , pp. 1-14
    • Chothia, C.1
  • 12
    • 0026665778 scopus 로고
    • Side-chain entropy oppose alpha-helix formation but rationalizes experimentally determined helix-forming propensities
    • Creamer, T. P. & Rose, G. D. (1992). Side-chain entropy oppose alpha-helix formation but rationalizes experimentally determined helix-forming propensities. Proc. Natl Acad. Sci. USA, 89, 5937-5941.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5937-5941
    • Creamer, T.P.1    Rose, G.D.2
  • 13
    • 2442481562 scopus 로고
    • Stability of folded conformations
    • Creighton, T. (1991). Stability of folded conformations. Curr. Opin. Struct. Biol. 1, 5-16.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 5-16
    • Creighton, T.1
  • 14
    • 0000589227 scopus 로고
    • Partitioning of nonpolar solutes into bilayers and amorphous n-alkanes
    • DeYoung, L. R. & Dill, K. A. (1990). Partitioning of nonpolar solutes into bilayers and amorphous n-alkanes. J. Phys. Chem. 94, 801-809.
    • (1990) J. Phys. Chem. , vol.94 , pp. 801-809
    • Deyoung, L.R.1    Dill, K.A.2
  • 15
    • 0027424690 scopus 로고
    • Molecular basis of cooperativity in protein folding: IV. CORE: A general cooperative folding model
    • Freire, E., Haynie, D. T. & Xie, D. (1993). Molecular basis of cooperativity in protein folding: IV. CORE: a general cooperative folding model. Proteins: Struct. Funct. Genet. 17, 111-123.
    • (1993) Proteins: Struct. Funct. Genet. , vol.17 , pp. 111-123
    • Freire, E.1    Haynie, D.T.2    Xie, D.3
  • 16
    • 0024638539 scopus 로고
    • Destabilization of an a-helical bundle by helix dipoles
    • Gilson, M. & Honig, B. (1989). Destabilization of an a-helical bundle by helix dipoles. Proc. Natl Acad. Sci. USA, 86, 1524-1528.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 1524-1528
    • Gilson, M.1    Honig, B.2
  • 17
    • 0014946546 scopus 로고
    • Molecular theory of the helix-coil transition in polyamino acids. II. Numerical evaluation of s and a for polyglycine and poly-L-alanine in the absence (for s and a) and presence (for a) of solvent
    • Go, M., Go, N. & Scheraga, H. A. (1970). Molecular theory of the helix-coil transition in polyamino acids. II. Numerical evaluation of s and a for polyglycine and poly-L-alanine in the absence (for s and a) and presence (for a) of solvent. J. Chem. Phys. 52, 2060-2079.
    • (1970) J. Chem. Phys. , vol.52 , pp. 2060-2079
    • Go, M.1    Go, N.2    Scheraga, H.A.3
  • 18
    • 51149216498 scopus 로고
    • Analysis of the contribution of internal vibrations to the statistical weights of equilibrium conformations of macromolecules
    • Go, N. & Scheraga, H. (1969). Analysis of the contribution of internal vibrations to the statistical weights of equilibrium conformations of macromolecules. J. Chem. Phys 51, 4751-4767.
    • (1969) J. Chem. Phys , vol.51 , pp. 4751-4767
    • Go, N.1    Scheraga, H.2
  • 19
    • 0014278260 scopus 로고
    • Molecular theory of the helix-coil transition in polyamino acids, I. Formulation
    • Go, N., Go, M. & Scheraga, H. A. (1968). Molecular theory of the helix-coil transition in polyamino acids, I. formulation. Proc. Natl Acad. Sci. USA, 59, 1030-1037.
    • (1968) Proc. Natl Acad. Sci. USA , vol.59 , pp. 1030-1037
    • Go, N.1    Go, M.2    Scheraga, H.A.3
  • 21
    • 0026748637 scopus 로고
    • Differential helix propensity of small apolar side-chains studied by molecular dynamics simulations
    • Hermans, J., Anderson, A. G. & Yun, Y. H. (1992). Differential helix propensity of small apolar side-chains studied by molecular dynamics simulations. Biochemistry, 31, 5646-5653.
    • (1992) Biochemistry , vol.31 , pp. 5646-5653
    • Hermans, J.1    Erson, A.G.2    Yun, Y.H.3
  • 22
    • 0028929583 scopus 로고
    • The free energy balance in protein folding
    • Honig, B. & Yang, A.-S. (1995). The free energy balance in protein folding. Advan. Protein Chem. 46, 27-58.
    • (1995) Advan. Protein Chem. , vol.46 , pp. 27-58
    • Honig, B.1    Yang, A.-S.2
  • 23
    • 33751385054 scopus 로고
    • Macroscopic models of aqueous solutions. Biological and chemical applications
    • Honig, B., Sharp, K. A. & Yang, A.-S. (1993). Macroscopic models of aqueous solutions. Biological and chemical applications. J. Phys. Chem. 97, 1101-1109.
    • (1993) J. Phys. Chem. , vol.97 , pp. 1101-1109
    • Honig, B.1    Sharp, K.A.2    Yang, A.-S.3
  • 24
    • 0000404146 scopus 로고
    • Size dependence of free energies. I. A Flory-Huggins approach
    • Kumar, S. K., Sharp, K., Rossky, P., Friedman, R. A. & Honig, B. (1995), Size dependence of free energies. I. A Flory-Huggins approach. J. Phys. Chem. 99, 8382-8391.
    • (1995) J. Phys. Chem. , vol.99 , pp. 8382-8391
    • Kumar, S.K.1    Sharp, K.2    Rossky, P.3    Friedman, R.A.4    Honig, B.5
  • 25
    • 0027305948 scopus 로고
    • Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration
    • Makhatadze, G. I. & Privalov, P. L. (1993). Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration. J. Mol. Biol. 232, 639-659.
    • (1993) J. Mol. Biol. , vol.232 , pp. 639-659
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 26
    • 0023461350 scopus 로고
    • Helix Stabilization by Glu- Lys+ salt bridges in short peptides of de novo design
    • Marqusee, S. & Baldwin, R. L. (1987). Helix Stabilization by Glu- Lys+ salt bridges in short peptides of de novo design. Proc. Natl Acad. Sci. USA, 84, 8898-8902.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 8898-8902
    • Marqusee, S.1    Baldwin, R.L.2
  • 27
    • 0024707204 scopus 로고
    • Unusually stable helix formation in short alanine-based peptides
    • Marqusee, S., Robbins, V. H. & Baldwin, R. L. (1989). Unusually stable helix formation in short alanine-based peptides. Proc. Natl. Acad. Sci. USA, 86, 5286-5290.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5286-5290
    • Marqusee, S.1    Robbins, V.H.2    Baldwin, R.L.3
  • 28
    • 33845377761 scopus 로고
    • Monte Carlo determination of the free energy and internal energy of hydration for the Ala dipeptide at 25°C
    • Mezei, M., Mehotra, P. K. & Beveridge, D. L. (1985). Monte Carlo determination of the free energy and internal energy of hydration for the Ala dipeptide at 25°C. J. Am. Chem. Soc. 107, 2239-2245.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2239-2245
    • Mezei, M.1    Mehotra, P.K.2    Beveridge, D.L.3
  • 29
    • 84986435971 scopus 로고
    • The nature of the N - H… O = C hydrogen bond: An intermolecular perturbation theory study of the formamide/formal-dehyde complex
    • Mitchell, J. B. O. & Price, S. L. (1990). The nature of the N - H… O = C hydrogen bond: an intermolecular perturbation theory study of the formamide/formal-dehyde complex. J. Comp. Chem. 11, 1217-1233.
    • (1990) J. Comp. Chem. , vol.11 , pp. 1217-1233
    • Mitchell, J.B.O.1    Price, S.L.2
  • 30
    • 0026344361 scopus 로고
    • Solid model compounds and the thermodynamics of protein unfolding
    • Murphy K. P. & Gill, S. J. (1991). Solid model compounds and the thermodynamics of protein unfolding. J. Mol. Biol. 222, 699-709.
    • (1991) J. Mol. Biol. , vol.222 , pp. 699-709
    • Murphy, K.P.1    Gill, S.J.2
  • 31
    • 0025098571 scopus 로고
    • Common features of protein unfolding and dissolution of hydrophobic compounds
    • Murphy K. P., Privalov, P. L. & Gill, S. J. (1990). Common features of protein unfolding and dissolution of hydrophobic compounds. Science, 247, 559-561.
    • (1990) Science , vol.247 , pp. 559-561
    • Murphy, K.P.1    Privalov, P.L.2    Gill, S.J.3
  • 32
    • 33947553005 scopus 로고
    • The structure of water and hydrophobic bonding in proteins. III. The thermodynamic properties of hydrophobic bonds in proteins
    • Nemethy G. & Scheraga, H. A. (1962). The structure of water and hydrophobic bonding in proteins. III. The thermodynamic properties of hydrophobic bonds in proteins. J. Phys. Chem. 66, 1773-1789.
    • (1962) J. Phys. Chem. , vol.66 , pp. 1773-1789
    • Nemethy, G.1    Scheraga, H.A.2
  • 33
    • 0015217634 scopus 로고
    • The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions
    • Nozaki, Y. & Tanford, C. H. (1971). The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. J. Biol. Chem. 246, 2211.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2211
    • Nozaki, Y.1    Tanford, C.H.2
  • 34
    • 0025877673 scopus 로고
    • Prediction of the thermodynamics of protein unfolding: The helix-coil transition of poly(L-alanine)
    • Ooi, T. & Oobatake, M. (1991). Prediction of the thermodynamics of protein unfolding: the helix-coil transition of poly(L-alanine). Proc. Natl Acad. Sci. USA, 88, 2859-2863.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2859-2863
    • Ooi, T.1    Oobatake, M.2
  • 35
    • 33947669512 scopus 로고
    • The potential of mean force surface for the alanine dipeptide in aqueous solution: A theoretical approach
    • Pettitt, B. M. & Karplus, M. (1985). The potential of mean force surface for the alanine dipeptide in aqueous solution: a theoretical approach. Chem. Phys. Letters, 121, 194.
    • (1985) Chem. Phys. Letters , vol.121 , pp. 194
    • Pettitt, B.M.1    Karplus, M.2
  • 36
    • 5544249775 scopus 로고
    • Conformational free energy of hydration for the alanine dipeptide: Thermodynamic analysis
    • Pettitt, B. M. & Karplus, M. (1988). Conformational free energy of hydration for the alanine dipeptide: thermodynamic analysis. J. Phys. Chem. 92, 3994-3997.
    • (1988) J. Phys. Chem. , vol.92 , pp. 3994-3997
    • Pettitt, B.M.1    Karplus, M.2
  • 37
    • 0000020527 scopus 로고
    • Helix-coil stability constants for the naturally occurring amino acids in water. IV. Alanine parameters from random poly(hydrox-ypropylglutamine-co-L-alanine)
    • Platzer, K. E. B., Ananthanarayanan, V. S., Andreatta, R. H. & Scheraga, H. A. (1972). Helix-coil stability constants for the naturally occurring amino acids in water. IV. alanine parameters from random poly(hydrox-ypropylglutamine-co-L-alanine).Macromoleculcs, 5, 177-187.
    • (1972) Macromoleculcs , vol.5 , pp. 177-187
    • Platzer, K.E.B.1    Ananthanarayanan, V.S.2    Reatta, R.H.3    Scheraga, H.A.4
  • 38
    • 0024290488 scopus 로고
    • Helix signals in proteins
    • Presta, L. G. & Rose, G. D. (1988). Helix signals in proteins. Science, 240, 1632-1641.
    • (1988) Science , vol.240 , pp. 1632-1641
    • Presta, L.G.1    Rose, G.D.2
  • 39
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov, P. & Gill, S. J. (1988). Stability of protein structure and hydrophobic interaction. Advan. Protein Chem. 39, 191-234.
    • (1988) Advan. Protein Chem. , vol.39 , pp. 191-234
    • Privalov, P.1    Gill, S.J.2
  • 40
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov, P. L. (1979). Stability of proteins: small globular proteins. Advan. Protein Chem. 33, 167-239.
    • (1979) Advan. Protein Chem. , vol.33 , pp. 167-239
    • Privalov, P.L.1
  • 41
    • 0027250627 scopus 로고
    • Contribution of hydration to protein folding thermodynamics. II The entropy and Gibbs energy of hydration
    • Privalov, P. L. & Makhatadze, G. I. (1993). Contribution of hydration to protein folding thermodynamics. II The entropy and Gibbs energy of hydration. J. Mol. Biol. 232, 660-679.
    • (1993) J. Mol. Biol. , vol.232 , pp. 660-679
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 42
    • 33751391161 scopus 로고
    • Helix-coil theories: A comparative study for finite length polypeptides
    • Qian, H. & Schellman, J. A. (1992). Helix-coil theories: a comparative study for finite length polypeptides. J. Phys. Chem. 96, 3987-3994.
    • (1992) J. Phys. Chem. , vol.96 , pp. 3987-3994
    • Qian, H.1    Schellman, J.A.2
  • 45
    • 0024836024 scopus 로고
    • A comparison of the CHARMM, AMBER, and ECEPP potentials for peptides. II f-y maps for N-acetyl alanine N'-methyl amide: Comparisons contrasts and simple experimental tests
    • Roterman, I. K., Lambert, M. H., Gibson, K. D. & Scheraga, H. A. (1989). A comparison of the CHARMM, AMBER, and ECEPP potentials for peptides. II f-y maps for N-acetyl alanine N'-methyl amide: comparisons contrasts and simple experimental tests. J. Biomol. Struct. Dynam. 7, 421-453.
    • (1989) J. Biomol. Struct. Dynam. , vol.7 , pp. 421-453
    • Roterman, I.K.1    Lambert, M.H.2    Gibson, K.D.3    Scheraga, H.A.4
  • 46
    • 77049276418 scopus 로고
    • The stability of hydrogen-bonded peptide structures in aqueous solution
    • Schellman, J. A. (1955). The stability of hydrogen-bonded peptide structures in aqueous solution. Trav. Lab. Carlsberg, Ser. Chim. 29, 230-259.
    • (1955) Trav. Lab. Carlsberg, Ser. Chim. , vol.29 , pp. 230-259
    • Schellman, J.A.1
  • 47
    • 33947476272 scopus 로고
    • The factors affecting the stability of hydrogen-bonded polypeptide structures in solution
    • Schellman, J. A. (1958). The factors affecting the stability of hydrogen-bonded polypeptide structures in solution. J. Phys. Chem. 62, 1485-1491.
    • (1958) J. Phys. Chem. , vol.62 , pp. 1485-1491
    • Schellman, J.A.1
  • 48
    • 84983617697 scopus 로고
    • A CFF91-base continuum solvation model: Solvation free energies of small organic molecules and conformations of the alanine dipeptides in solution
    • Schmidt, A. B. & Fine, R. M. (1995). A CFF91-base continuum solvation model: solvation free energies of small organic molecules and conformations of the alanine dipeptides in solution. Mol. Sim. In the press.
    • (1995) Mol. Sim
    • Schmidt, A.B.1    Fine, R.M.2
  • 50
    • 0025849701 scopus 로고
    • Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water
    • Scholtz, J. M., Marquess, S., Baldwin, R. L., York, E. J., Stewart, J. M., Santoro, M. & Bolen, D. W. (1991). Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water. Proc. Natl Acad. Sci. USA, 88, 2854-2858.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2854-2858
    • Scholtz, J.M.1    Marquess, S.2    Baldwin, R.L.3    York, E.J.4    Stewart, J.M.5    Santoro, M.6    Bolen, D.W.7
  • 51
    • 0027497118 scopus 로고
    • The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide
    • Scholtz, J. M., Qian, H., Robbins, V. H. & Baldwin, R. L. (1993). The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide. Biochemistry, 32, 9668-9676.
    • (1993) Biochemistry , vol.32 , pp. 9668-9676
    • Scholtz, J.M.1    Qian, H.2    Robbins, V.H.3    Baldwin, R.L.4
  • 52
    • 0026516310 scopus 로고
    • Effect of alanine versus glycine in a-helices on protein stability
    • Serrano, L., Neira, J., Sancho, J. & Fersht, A. (1992). Effect of alanine versus glycine in a-helices on protein stability Nature, 356, 453-455.
    • (1992) Nature , vol.356 , pp. 453-455
    • Serrano, L.1    Neira, J.2    Sancho, J.3    Fersht, A.4
  • 53
    • 0026076664 scopus 로고
    • Extracting hydrophobic free energies from experimental data: Relationship to protein folding and theoretical models
    • Sharp, K. A., Nicholls, A., Friedman, R. & Honig, B. (1991). Extracting hydrophobic free energies from experimental data: relationship to protein folding and theoretical models. Biochemistry, 30, 9686-9697.
    • (1991) Biochemistry , vol.30 , pp. 9686-9697
    • Sharp, K.A.1    Nicholls, A.2    Friedman, R.3    Honig, B.4
  • 54
    • 0026584344 scopus 로고
    • Contribution of hydrogen bonding to the conforma-tiona stability of ribonuclease T1
    • Shirley B. A., Stanssens, P., Hahn, U. & Pace, C. N. (1992). Contribution of hydrogen bonding to the conforma-tiona stability of ribonuclease T1. Biochemistry, 31, 725-732.
    • (1992) Biochemistry , vol.31 , pp. 725-732
    • Shirley, B.A.1    Stanssens, P.2    Hahn, U.3    Pace, C.N.4
  • 55
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic solvent models
    • Sitkoff, D., Sharp, K. A. & Honig, B. (1994). Accurate calculation of hydration free energies using macroscopic solvent models. J. Phys. Chem. 98, 1978-1988.
    • (1994) J. Phys. Chem. , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 56
    • 0342809856 scopus 로고
    • Conformational equilibrium in the alanine dipeptide in the gas phase and aqueous solution: A comparison of theoretical results
    • Tobias, D. J. & Brooks, C. L. (1992). Conformational equilibrium in the alanine dipeptide in the gas phase and aqueous solution: a comparison of theoretical results. J. Phys. Chem. 96, 3864-3870.
    • (1992) J. Phys. Chem. , vol.96 , pp. 3864-3870
    • Tobias, D.J.1    Brooks, C.L.2
  • 57
    • 0025767212 scopus 로고
    • Thermodynamics and mechanism of a helix inititation in alanine and valine peptides
    • Tobias, D. L. & Brooks, C. L. (1991). Thermodynamics and mechanism of a helix inititation in alanine and valine peptides. Biochemistry, 30, 6059-6070.
    • (1991) Biochemistry , vol.30 , pp. 6059-6070
    • Tobias, D.L.1    Brooks, C.L.2
  • 58
    • 0023673867 scopus 로고
    • Effect of sequence-specific interactions on the stability of helical conformations in polypeptides
    • Vasquez, M. & 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
    • Vasquez, M.1    Scheraga, H.A.2
  • 59
    • 0023297091 scopus 로고
    • Helix-coil transition theory including long-range electrostatic interactions: Application to globular proteins
    • Vasquez, M., Pincus, M. R. & Scheraga, H. A. (1987). Helix-coil transition theory including long-range electrostatic interactions: application to globular proteins. Biopolymers, 26, 351-371.
    • (1987) Biopolymers , vol.26 , pp. 351-371
    • Vasquez, M.1    Pincus, M.R.2    Scheraga, H.A.3
  • 60
    • 0026076082 scopus 로고
    • Empirical solvation models can be used to differentiate native from near-native conformations of bovine pancreatic trypsin, inhibitor
    • Vila, J., Williams, R., Vasquez, M. & Scheraga, H. A. (1991). Empirical solvation models can be used to differentiate native from near-native conformations of bovine pancreatic trypsin, inhibitor. Proteins: Struct. Funct. Genet. 10, 199-218.
    • (1991) Proteins: Struct. Funct. Genet. , vol.10 , pp. 199-218
    • Vila, J.1    Williams, R.2    Vasquez, M.3    Scheraga, H.A.4
  • 62
    • 0027080909 scopus 로고
    • Atomic solvation parameters applied to molecular dynamics ofproteins in solution
    • Wesson, L. & Eisenberg, D. (1992). Atomic solvation parameters applied to molecular dynamics ofproteins in solution. Protein Sci. 1, 227-235.
    • (1992) Protein Sci , vol.1 , pp. 227-235
    • Wesson, L.1    Eisenberg, D.2
  • 63
    • 0025082921 scopus 로고
    • Helix-coil stability constants for the naturally occuring amino acids in water. XXIV Halh-cystine parameters from random poly(hydroxybutylglu-tamine-co-S-methylthio-L-cystine)
    • Wojcik, J., Altmann, K.-H. & Scheraga, H. A. (1990). Helix-coil stability constants for the naturally occuring amino acids in water. XXIV Halh-cystine parameters from random poly(hydroxybutylglu-tamine-co-S-methylthio-L-cystine). Biopolymers, 30, 107-120.
    • (1990) Biopolymers , vol.30 , pp. 107-120
    • Wojcik, J.1    Altmann, K.-H.2    Scheraga, H.A.3
  • 64
    • 0017855698 scopus 로고
    • Interaction of the peptide bond with solvent water: A vapor phase analysis
    • Wolfenden, R. (1978). Interaction of the peptide bond with solvent water: a vapor phase analysis. Biochemistry, 17, 199-204.
    • (1978) Biochemistry , vol.17 , pp. 199-204
    • Wolfenden, R.1
  • 65
    • 0026800672 scopus 로고
    • Analysis of the heat capacity dependence of protein folding
    • Yang, A.-S., Sharp, K. & Honig, B. (1992). Analysis of the heat capacity dependence of protein folding. J. Mol. Biol. 227, 889-900.
    • (1992) J. Mol. Biol. , vol.227 , pp. 889-900
    • Yang, A.-S.1    Sharp, K.2    Honig, B.3
  • 66
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm, B. H. & Bragg, J. K. (1959). Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31, 526-535.
    • (1959) J. Chem. Phys. , vol.31 , pp. 526-535
    • Zimm, B.H.1    Bragg, J.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.