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Volumn 85, Issue 1, 2000, Pages 25-39

Heat capacity of hydrogen-bonded networks: An alternative view of protein folding thermodynamics

Author keywords

Heat capacity; Hydrogen bond network; Protein folding thermodynamics

Indexed keywords

ARTICLE; ENTHALPY; ENTROPY; HYDROGEN BOND; HYDROPHOBICITY; MELTING POINT; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN FOLDING; THERMODYNAMICS;

EID: 0034738021     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(00)00136-8     Document Type: Article
Times cited : (133)

References (52)
  • 1
    • 0014963345 scopus 로고
    • Thermodynamics of protein denaturation. Calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation
    • Jackson W.M., Brandts J.F. Thermodynamics of protein denaturation. Calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation. Biochemistry. 9:1970;2294-2301.
    • (1970) Biochemistry , vol.9 , pp. 2294-2301
    • Jackson, W.M.1    Brandts, J.F.2
  • 2
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov P.L. Stability of proteins: small globular proteins. Adv. Protein Chem. 33:1979;167-241.
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 3
    • 0000826487 scopus 로고
    • Biochemical applications of differential scanning calorimetry
    • Sturtevant J.M. Biochemical applications of differential scanning calorimetry. Ann. Rev. Phys. Chem. 38:1987;463-488.
    • (1987) Ann. Rev. Phys. Chem. , vol.38 , pp. 463-488
    • Sturtevant, J.M.1
  • 4
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interactions
    • Privalov P.L., Gill S.J. Stability of protein structure and hydrophobic interactions. Adv. Protein Chem. 39:1988;191-234.
    • (1988) Adv. Protein Chem. , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 5
    • 0025287103 scopus 로고
    • Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins
    • Privalov P.L., Makhatadze G.I. Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins. J. Mol. Biol. 213:1990;385-391.
    • (1990) J. Mol. Biol. , vol.213 , pp. 385-391
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 6
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill K.A. Dominant forces in protein folding. Biochemistry. 29:1990;7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 7
    • 0037920996 scopus 로고    scopus 로고
    • Thermodynamics of protein folding and stability
    • G. Allen. Stamford, CT: JAI Press Inc
    • Cooper A. Thermodynamics of protein folding and stability. Allen G. Protein: A Comprehensive Treatise, vol. 2. 1999;217-270 JAI Press Inc, Stamford, CT.
    • (1999) Protein: A Comprehensive Treatise, Vol. 2 , pp. 217-270
    • Cooper, A.1
  • 8
    • 0037943192 scopus 로고    scopus 로고
    • A new set of peptide-based group heat capacities for use in protein stability calculations
    • Häckel M., Hinz H-J., Hedwig G.R. A new set of peptide-based group heat capacities for use in protein stability calculations. J. Mol. Biol. 291:1999;197-213.
    • (1999) J. Mol. Biol. , vol.291 , pp. 197-213
    • Häckel, M.1    Hinz, H.-J.2    Hedwig, G.R.3
  • 9
    • 33748600422 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of dissociation of ligand-induced dimers of vancomycin antibiotics
    • McPhail D., Cooper A. Thermodynamics and kinetics of dissociation of ligand-induced dimers of vancomycin antibiotics. J. Chem. Soc. Faraday Trans. 93:1997;2283-2289.
    • (1997) J. Chem. Soc. Faraday Trans. , vol.93 , pp. 2283-2289
    • McPhail, D.1    Cooper, A.2
  • 10
    • 0032850996 scopus 로고    scopus 로고
    • Thermodynamic analysis of biomolecular interactions
    • Cooper A. Thermodynamic analysis of biomolecular interactions. Curr. Opin. Chem. Biol. 3:1999;557-563.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 557-563
    • Cooper, A.1
  • 11
    • 0029395478 scopus 로고
    • Win some, lose some: Enthalpy-entropy compensation in weak intermolecular interactions
    • Dunitz J.D. Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions. Chem. Biol. 2:1995;709-712.
    • (1995) Chem. Biol. , vol.2 , pp. 709-712
    • Dunitz, J.D.1
  • 12
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W. Some factors in the interpretation of protein denaturation. Adv. Protein Chem. 14:1959;1-63.
    • (1959) Adv. Protein Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 14
    • 0026684671 scopus 로고
    • Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water
    • Spolar R.S., Livingstone J.R., Record M.T. Jr. Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water. Biochemistry. 31:1992;3947-3955.
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar, R.S.1    Livingstone, J.R.2    Record M.T., Jr.3
  • 15
    • 0029094346 scopus 로고
    • Enthalpic contributions to protein stability: Insights from atom-based calculations and statistical mechanics
    • Lazaridis T., Archontis G., Karplus M. Enthalpic contributions to protein stability: insights from atom-based calculations and statistical mechanics. Adv. Protein Chem. 47:1995;231-306.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 231-306
    • Lazaridis, T.1    Archontis, G.2    Karplus, M.3
  • 16
    • 0032994570 scopus 로고    scopus 로고
    • Protein heat capacity: Inconsistencies in the current view of cold denaturation
    • Hallerbach B., Hinz H.-J. Protein heat capacity: inconsistencies in the current view of cold denaturation. Biophys. Chem. 76:1999;219-227.
    • (1999) Biophys. Chem. , vol.76 , pp. 219-227
    • Hallerbach, B.1    Hinz, H.-J.2
  • 17
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • Pace C.N., Shirley B.N., McNutt M., Gajiwala K. Forces contributing to the conformational stability of proteins. FASEB J. 10:1996;75-83.
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.N.2    McNutt, M.3    Gajiwala, K.4
  • 18
    • 0029843132 scopus 로고    scopus 로고
    • Hydrogen bonding stabilises globular proteins
    • Myers J.K., Pace C.N. Hydrogen bonding stabilises globular proteins. Biophys. J. 71:1996;2033-2039.
    • (1996) Biophys. J. , vol.71 , pp. 2033-2039
    • Myers, J.K.1    Pace, C.N.2
  • 19
    • 0027256739 scopus 로고
    • Hydrogen-bonding, hydrophobicity, packing and protein folding
    • Rose G.D., Wolfenden R. Hydrogen-bonding, hydrophobicity, packing and protein folding. Annu. Rev. Biophys. Biomol. Struct. 22:1993;381-415.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 381-415
    • Rose, G.D.1    Wolfenden, R.2
  • 20
    • 0008136430 scopus 로고    scopus 로고
    • Heat capacities and entropies of organic compounds in the condensed phase. Volume III
    • Domalski E.S., Hearing E.D. Heat capacities and entropies of organic compounds in the condensed phase. Volume III. J. Phys. Chem. Ref. Data. 25:1996;1-525.
    • (1996) J. Phys. Chem. Ref. Data , vol.25 , pp. 1-525
    • Domalski, E.S.1    Hearing, E.D.2
  • 21
    • 0001234019 scopus 로고
    • A group additivity approach for the estimation of heat capacities of organic liquids and solids at 298 K
    • Chickos J.S., Hesse D.G., Liebman J.F. A group additivity approach for the estimation of heat capacities of organic liquids and solids at 298 K. Struct. Chem. 4:1993;261-269.
    • (1993) Struct. Chem. , vol.4 , pp. 261-269
    • Chickos, J.S.1    Hesse, D.G.2    Liebman, J.F.3
  • 23
    • 0015977588 scopus 로고
    • The interpretation of protein structures: Total volume, group volume distributions and packing density
    • Richards F.M. The interpretation of protein structures: total volume, group volume distributions and packing density. J. Mol. Biol. 82:1974;1-14.
    • (1974) J. Mol. Biol. , vol.82 , pp. 1-14
    • Richards, F.M.1
  • 24
    • 0000725483 scopus 로고
    • Thermodynamic fluctuations in protein molecules
    • Cooper A. Thermodynamic fluctuations in protein molecules. Proc. Natl. Acad. Sci. USA. 73:1976;2740-2741.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2740-2741
    • Cooper, A.1
  • 25
    • 0033516705 scopus 로고    scopus 로고
    • The packing density in proteins: Standard radii and volumes
    • Tsai J., Taylor R., Chothia C., Gerstein M. The packing density in proteins: standard radii and volumes. J. Mol. Biol. 290:1999;253-266.
    • (1999) J. Mol. Biol. , vol.290 , pp. 253-266
    • Tsai, J.1    Taylor, R.2    Chothia, C.3    Gerstein, M.4
  • 26
    • 0033613906 scopus 로고    scopus 로고
    • Native proteins are surface molten solids: Application of the Lindemann criterion for solid versus liquid state
    • Zhou Y., Vitkup D., Karplus M. Native proteins are surface molten solids: application of the Lindemann criterion for solid versus liquid state. J. Mol. Biol. 285:1999;1371-1375.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1371-1375
    • Zhou, Y.1    Vitkup, D.2    Karplus, M.3
  • 27
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald I.K., Thornton J.M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238:1994;777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 29
    • 0032860932 scopus 로고    scopus 로고
    • Local water bridges and protein conformational stability
    • Petukhov M., Cregut D., Soares C.M., Serrano L. Local water bridges and protein conformational stability. Protein Sci. 8:1999;1982-1989.
    • (1999) Protein Sci. , vol.8 , pp. 1982-1989
    • Petukhov, M.1    Cregut, D.2    Soares, C.M.3    Serrano, L.4
  • 30
    • 0342331607 scopus 로고    scopus 로고
    • Eccentricities of an everyday substance (book review)
    • Stillinger F.H. Eccentricities of an everyday substance (book review). Nature. 401:1999;850-851.
    • (1999) Nature , vol.401 , pp. 850-851
    • Stillinger, F.H.1
  • 31
    • 0014356189 scopus 로고
    • Stability of an amide-hydrogen bond in an apolar environment
    • Klotz I.M., Farnham S.B. Stability of an amide-hydrogen bond in an apolar environment. Biochemistry. 7:1968;3879-3882.
    • (1968) Biochemistry , vol.7 , pp. 3879-3882
    • Klotz, I.M.1    Farnham, S.B.2
  • 32
    • 0014448561 scopus 로고
    • The thermodynamics of transfer of amides from an apolar to an aqueous solution
    • Kresheck G.C., Klotz I.M. The thermodynamics of transfer of amides from an apolar to an aqueous solution. Biochemistry. 8:1969;8-12.
    • (1969) Biochemistry , vol.8 , pp. 8-12
    • Kresheck, G.C.1    Klotz, I.M.2
  • 33
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behavior in proteins
    • Murphy K.P., Freire E. Thermodynamics of structural stability and cooperative folding behavior in proteins. Adv. Protein Chem. 43:1992;313-361.
    • (1992) Adv. Protein Chem. , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 35
    • 0033550298 scopus 로고    scopus 로고
    • The cooperativity of burst phase reactions explored
    • Parker M.J., Marqusee S. The cooperativity of burst phase reactions explored. J. Mol. Biol. 293:1999;1195-1210.
    • (1999) J. Mol. Biol. , vol.293 , pp. 1195-1210
    • Parker, M.J.1    Marqusee, S.2
  • 37
    • 0028925570 scopus 로고
    • Protein destabilization at low temperatures
    • Franks F. Protein destabilization at low temperatures. Adv. Protein Chem. 46:1995;105-139.
    • (1995) Adv. Protein Chem. , vol.46 , pp. 105-139
    • Franks, F.1
  • 38
    • 0029941271 scopus 로고    scopus 로고
    • Energetics of hydrogen bonding in proteins: A model compound study
    • Habermann S.M., Murphy K.P. Energetics of hydrogen bonding in proteins: a model compound study. Protein Sci. 5:1996;1229-1239.
    • (1996) Protein Sci. , vol.5 , pp. 1229-1239
    • Habermann, S.M.1    Murphy, K.P.2
  • 41
    • 0032550183 scopus 로고    scopus 로고
    • Heat capacities of amino acids, peptides and proteins
    • Makhatadze G.I. Heat capacities of amino acids, peptides and proteins. Biophys. Chem. 71:1998;133-156.
    • (1998) Biophys. Chem. , vol.71 , pp. 133-156
    • Makhatadze, G.I.1
  • 42
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • Baldwin R.L. Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl. Acad. Sci. USA. 83:1986;8069-8072.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8069-8072
    • Baldwin, R.L.1
  • 43
    • 0026018045 scopus 로고
    • Isoenthalpic and isoentropic temperatures and the thermodynamics of protein denaturation
    • Lee B. Isoenthalpic and isoentropic temperatures and the thermodynamics of protein denaturation. Proc. Natl. Acad. Sci. USA. 88:1991;5154-5158.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5154-5158
    • Lee, B.1
  • 44
    • 0025098571 scopus 로고
    • Common features of protein unfolding and dissolution of hydrophobic compounds
    • Murphy K.P., Privalov P.L., Gill S.J. Common features of protein unfolding and dissolution of hydrophobic compounds. Science. 247:1990;559-561.
    • (1990) Science , vol.247 , pp. 559-561
    • Murphy, K.P.1    Privalov, P.L.2    Gill, S.J.3
  • 45
    • 0031561809 scopus 로고    scopus 로고
    • Protein binding versus protein folding: The role of hydrophilic bridges in protein associations
    • Xu D., Lin S.L., Nussinov R. Protein binding versus protein folding: the role of hydrophilic bridges in protein associations. J. Mol. Biol. 265:1997;68-84.
    • (1997) J. Mol. Biol. , vol.265 , pp. 68-84
    • Xu, D.1    Lin, S.L.2    Nussinov, R.3
  • 46
    • 0032489503 scopus 로고    scopus 로고
    • Thermodynamic characterization of non-sequence-specific DNA-binding by the Sso7d protein from Sulfolobus solfataricus
    • Lundbäck T., Hansson H., Knapp S., Ladenstein R., Härd T. Thermodynamic characterization of non-sequence-specific DNA-binding by the Sso7d protein from Sulfolobus solfataricus. J. Mol. Biol. 276:1998;775-786.
    • (1998) J. Mol. Biol. , vol.276 , pp. 775-786
    • Lundbäck, T.1    Hansson, H.2    Knapp, S.3    Ladenstein, R.4    Härd, T.5
  • 47
    • 0032507251 scopus 로고    scopus 로고
    • Origin of β-hairpin stability in solution: Structural and thermodynamic analysis of the folding of a model peptide supports hydrophobic stabilization in water
    • Maynard A.J., Sharman G.J., Searle M.S. Origin of β-hairpin stability in solution: structural and thermodynamic analysis of the folding of a model peptide supports hydrophobic stabilization in water. J. Am. Chem. Soc. 120:1998;1996-2007.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 1996-2007
    • Maynard, A.J.1    Sharman, G.J.2    Searle, M.S.3
  • 48
    • 0033609809 scopus 로고    scopus 로고
    • A calorimetric study of the folding-unfolding of an α-helix with covalently closed N and C-terminal loops
    • Taylor J.W., Greenfield N.J., Wu B., Privalov P.L. A calorimetric study of the folding-unfolding of an α-helix with covalently closed N and C-terminal loops. J. Mol. Biol. 291:1999;965-976.
    • (1999) J. Mol. Biol. , vol.291 , pp. 965-976
    • Taylor, J.W.1    Greenfield, N.J.2    Wu, B.3    Privalov, P.L.4
  • 50
    • 0034719388 scopus 로고    scopus 로고
    • Design of single-layer β-sheets without a hydrophobic core
    • Kolde S., Huang X., Link K., Koide A., Bu Z., Engelman D.M. Design of single-layer β-sheets without a hydrophobic core. Nature. 403:2000;456-460.
    • (2000) Nature , vol.403 , pp. 456-460
    • Kolde, S.1    Huang, X.2    Link, K.3    Koide, A.4    Bu, Z.5    Engelman, D.M.6


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