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Volumn 313, Issue 3-4, 2002, Pages 540-548

Heat capacities of solid state proteins: Implications for protein stability in solution

Author keywords

Heat capacity; Protein; Solid state; Vibrational modes

Indexed keywords

HYDRATION; MOLECULAR VIBRATIONS; SOLUTIONS; SPECIFIC HEAT; THERMAL EFFECTS;

EID: 0037107949     PISSN: 03784371     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-4371(02)00997-4     Document Type: Article
Times cited : (4)

References (27)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science. 181:1973;223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 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
  • 4
    • 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
  • 5
    • 0025360593 scopus 로고
    • Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: Hydration effect
    • Makhatadze G.I., Privalov P.L. Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution. hydration effect J. Mol. Biol. 213:1990;375-384.
    • (1990) J. Mol. Biol. , vol.213 , pp. 375-384
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 6
    • 0026511652 scopus 로고
    • Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding
    • Privalov P.L., Makhatadze G.I. Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding. J. Mol. Biol. 224:1992;715-723.
    • (1992) J. Mol. Biol. , vol.224 , pp. 715-723
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 7
    • 0027305948 scopus 로고
    • Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration
    • Makhatadze G.I., Privalov P.L. Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration. J. Mol. Biol. 232:1993;639-659.
    • (1993) J. Mol. Biol. , vol.232 , pp. 639-659
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 8
    • 0027250627 scopus 로고
    • Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration
    • Privalov P.L., Makhatadze G.I. Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration. J. Mol. Biol. 232:1993;660-679.
    • (1993) J. Mol. Biol. , vol.232 , pp. 660-679
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 9
    • 0014669266 scopus 로고
    • Heat capacities from 11 to 305° K and entropies of hydrated and anhydrous bovine zinc insulin and bovine chymotrypsinogen A
    • Hutchens J.O., Cole A.G., Stout J.W. Heat capacities from 11 to. 305° K and entropies of hydrated and anhydrous bovine zinc insulin and bovine chymotrypsinogen A J. Biol. Chem. 244:1969;26-32.
    • (1969) J. Biol. Chem. , vol.244 , pp. 26-32
    • Hutchens, J.O.1    Cole, A.G.2    Stout, J.W.3
  • 10
    • 0015176914 scopus 로고
    • Calorimetry of rat tail tendon collagen before and after denaturation: The heat of fusion of its absorbed water
    • A.R. Haly, J.W. Snaith, Calorimetry of rat tail tendon collagen before and after denaturation: the heat of fusion of its absorbed water, Biopolymers 10 (1971) 1681-1699.
    • (1971) Biopolymers , vol.10 , pp. 1681-1699
    • Haly, A.R.1    Snaith, J.W.2
  • 11
    • 0017099930 scopus 로고
    • Thermal properties of collagen in helical and random coiled states in the temperature range from 4° K to 300° K
    • Andronikashvili E.L., Mrevlishvili G.M., Japaridze G.Sh., Sokhadze V.M., Kvavadze K.A. Thermal properties of collagen in helical and random coiled states in the temperature range from. 4° K to 300° K Biopolymers. 15:1976;1991-2004.
    • (1976) Biopolymers , vol.15 , pp. 1991-2004
    • Andronikashvili, E.L.1    Mrevlishvili, G.M.2    Japaridze, G.Sh.3    Sokhadze, V.M.4    Kvavadze, K.A.5
  • 12
    • 84926521598 scopus 로고
    • The ATHAS database on heat capacities of polymers
    • Wunderlich B. The ATHAS database on heat capacities of polymers. Pure Appl. Chem. 67:1995;1019-1026.
    • (1995) Pure Appl. Chem. , vol.67 , pp. 1019-1026
    • Wunderlich, B.1
  • 15
    • 0003031632 scopus 로고
    • Heat capacities of linear high polymers
    • Wunderlich B., Baur H. Heat capacities of linear high polymers. Adv. Polym. Sci. 7:1970;151-368.
    • (1970) Adv. Polym. Sci. , vol.7 , pp. 151-368
    • Wunderlich, B.1    Baur, H.2
  • 16
    • 0003690919 scopus 로고
    • Academic Press, London, UK (Chapter 5)
    • Wunderlich B. Thermal Analysis. 1990;Academic Press, London, UK. (Chapter 5).
    • (1990) Thermal Analysis
    • Wunderlich, B.1
  • 17
  • 18
    • 0030262602 scopus 로고    scopus 로고
    • A new method of fitting approximate vibrational spectra to heat capacities of solids with Tarasov functions
    • Ge Zhang, B. Wunderlich, A new method of fitting approximate vibrational spectra to heat capacities of solids with Tarasov functions, J. Therm. Anal. 47 (1996) 899-911.
    • (1996) J. Therm. Anal. , vol.47 , pp. 899-911
    • Zhang, G.1    Wunderlich, B.2
  • 21
    • 0037083891 scopus 로고    scopus 로고
    • Specific heat upon aqueous unfolding of the protein interior: A theoretical approach
    • A. Bakk, J.S. Høye, A. Hansen, Specific heat upon aqueous unfolding of the protein interior: a theoretical approach, Physica A 304 (2002) 355-361.
    • (2002) Physica A , vol.304 , pp. 355-361
    • Bakk, A.1    Høye, J.S.2    Hansen, A.3
  • 22
    • 0036154172 scopus 로고    scopus 로고
    • Apolar and polar solvation thermodynamics related to the protein unfolding process
    • Bakk A., H ø ye J.S., Hansen A. Apolar and polar solvation thermodynamics related to the protein unfolding process. Biophys. J. 82:2002;713-719.
    • (2002) Biophys. J. , vol.82 , pp. 713-719
    • Bakk, A.1    Høye, J.S.2    Hansen, A.3
  • 25
    • 0024977331 scopus 로고
    • Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies
    • B.-lu. Chen, J.A. Schellman, Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies, Biochemistry USA 28 (1989) 685-691.
    • (1989) Biochemistry USA , vol.28 , pp. 685-691
    • Chen, B.-Lu.1    Schellman, J.A.2
  • 26
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.