메뉴 건너뛰기




Volumn 6, Issue 1, 1997, Pages 222-232

Temperature dependence of the preferential interactions of ribonuclease A in aqueous co-solvent systems: Thermodynamic analysis

Author keywords

preferential binding; protein stabilization by co solvents; protein solvent interactions; transfer enthalpy; transfer free energy

Indexed keywords

RIBONUCLEASE A;

EID: 0031022452     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060124     Document Type: Article
Times cited : (62)

References (37)
  • 2
    • 0025068721 scopus 로고
    • Why preferential hydration does not always stabilize the native structure of globular proteins
    • Arakawa T, Bhat R, Timasheff SN. 1990b. Why preferential hydration does not always stabilize the native structure of globular proteins. Biochemistry 29:1924-1931.
    • (1990) Biochemistry , vol.29 , pp. 1924-1931
    • Arakawa, T.1    Bhat, R.2    Timasheff, S.N.3
  • 3
    • 0021755248 scopus 로고
    • Mechanism of protein salting in and salting out by divalent cation salts: Balance between hydration and salt binding
    • Arakawa T, Timasheff SN. 1984a. Mechanism of protein salting in and salting out by divalent cation salts: Balance between hydration and salt binding. Biochemistry 23:5912-5923.
    • (1984) Biochemistry , vol.23 , pp. 5912-5923
    • Arakawa, T.1    Timasheff, S.N.2
  • 4
    • 0021755210 scopus 로고
    • Protein stabilization and destabilization by guanidinium salts
    • Arakawa T, Timasheff SN. 1984b. Protein stabilization and destabilization by guanidinium salts. Biochemistry 23:5924-5929.
    • (1984) Biochemistry , vol.23 , pp. 5924-5929
    • Arakawa, T.1    Timasheff, S.N.2
  • 5
    • 0014681206 scopus 로고
    • Studies of the chymotrypsinogen family of proteins. VII. Thermodynamic analysis of transition I of α-chymotrypsin
    • Biltonen R, Lumry R. 1969. Studies of the chymotrypsinogen family of proteins. VII. Thermodynamic analysis of transition I of α-chymotrypsin. J Am Chem Soc 91:4256-4264.
    • (1969) J Am Chem Soc , vol.91 , pp. 4256-4264
    • Biltonen, R.1    Lumry, R.2
  • 6
    • 0039692420 scopus 로고
    • Osmotic and activity coefficients of sodium chloride-sorbitol and potassium chloride-sorbitol solutions at 25 °C
    • Bonner OD. 1982. Osmotic and activity coefficients of sodium chloride-sorbitol and potassium chloride-sorbitol solutions at 25 °C. J Solution Chemistry 11:315-324.
    • (1982) J Solution Chemistry , vol.11 , pp. 315-324
    • Bonner, O.D.1
  • 7
    • 0014349173 scopus 로고
    • Protein hydration. 1. Binding sites
    • Bull HB, Breese K. 1968. Protein hydration. 1. Binding sites. Arch Biochem Biophys 128:488-496.
    • (1968) Arch Biochem Biophys , vol.128 , pp. 488-496
    • Bull, H.B.1    Breese, K.2
  • 8
    • 33947475430 scopus 로고
    • Partial specific volumes and refractive index increments in multicomponent systems
    • Casassa EF, Eisenberg H. 1961. Partial specific volumes and refractive index increments in multicomponent systems. J Phys Chem 65:427-433.
    • (1961) J Phys Chem , vol.65 , pp. 427-433
    • Casassa, E.F.1    Eisenberg, H.2
  • 9
    • 77956752195 scopus 로고
    • Thermodynamic analysis of multicomponent solutions
    • Casassa EF, Eisenberg H. 1964. Thermodynamic analysis of multicomponent solutions. Adv Protein Chem 19:287-395.
    • (1964) Adv Protein Chem , vol.19 , pp. 287-395
    • Casassa, E.F.1    Eisenberg, H.2
  • 10
    • 0014231119 scopus 로고
    • Deoxyribonucleate solutions: Sedimentation in a density gradient, partial specific volumes, density and refractive index increments, and preferential interactions
    • Cohen G, Eisenberg H. 1968. Deoxyribonucleate solutions: Sedimentation in a density gradient, partial specific volumes, density and refractive index increments, and preferential interactions. Biopolymers 6:1077-1100.
    • (1968) Biopolymers , vol.6 , pp. 1077-1100
    • Cohen, G.1    Eisenberg, H.2
  • 11
    • 0022147096 scopus 로고
    • The Hofmeister effect and the behaviour of water at interfaces
    • Collins KD, Washabaugh MW. 1985. The Hofmeister effect and the behaviour of water at interfaces. Q Rev Biophys 18:323-422.
    • (1985) Q Rev Biophys , vol.18 , pp. 323-422
    • Collins, K.D.1    Washabaugh, M.W.2
  • 12
    • 0019585856 scopus 로고
    • Preferential hydration of bovine serum albumin in polyhydric alcohol-water mixtures
    • Gekko K, Morikawa T. 1981a. Preferential hydration of bovine serum albumin in polyhydric alcohol-water mixtures. J Biochem 90:39-50.
    • (1981) J Biochem , vol.90 , pp. 39-50
    • Gekko, K.1    Morikawa, T.2
  • 13
    • 0019590230 scopus 로고
    • Thermodynamics of polyol-induced thermal stabilization of chymotrypsinogen
    • Gekko K, Morikawa T. 1981b. Thermodynamics of polyol-induced thermal stabilization of chymotrypsinogen. J Biochem 90:51-60.
    • (1981) J Biochem , vol.90 , pp. 51-60
    • Gekko, K.1    Morikawa, T.2
  • 14
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures
    • Gekko K, Timasheff SN. 1981. Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures. Biochemistry 20:4667-4676.
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 16
    • 0015257703 scopus 로고
    • Preferential and absolute interactions of solvent components with proteins in mixed solvent systems
    • Inoue H, Timasheff SN. 1972. Preferential and absolute interactions of solvent components with proteins in mixed solvent systems. Biopolymers 11:737-743.
    • (1972) Biopolymers , vol.11 , pp. 737-743
    • Inoue, H.1    Timasheff, S.N.2
  • 17
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W. 1959. Some factors in the interpretation of protein denaturation. Adv Protein Chem 14:1-63.
    • (1959) Adv Protein Chem , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 19
    • 0000800911 scopus 로고
    • Hydration of macromolecules. III. Hydration of polypeptides
    • Kuntz ID. 1971. Hydration of macromolecules. III. Hydration of polypeptides. J Am Chem Soc 93:514-516.
    • (1971) J Am Chem Soc , vol.93 , pp. 514-516
    • Kuntz, I.D.1
  • 20
    • 0016022523 scopus 로고
    • Hydration of proteins and polypeptides
    • Kuntz ID, Kauzmann W. 1974. Hydration of proteins and polypeptides. Adv Protein Chem 28:239-345.
    • (1974) Adv Protein Chem , vol.28 , pp. 239-345
    • Kuntz, I.D.1    Kauzmann, W.2
  • 22
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • Lee JC, Timasheff SN. 1981. The stabilization of proteins by sucrose. J Biol Chem 256:7193-7201.
    • (1981) J Biol Chem , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 23
    • 0028862864 scopus 로고
    • The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
    • Liu Y, Bolen DS. 1995. The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. Biochemistry 34:12884-12891.
    • (1995) Biochemistry , vol.34 , pp. 12884-12891
    • Liu, Y.1    Bolen, D.S.2
  • 24
    • 0017598226 scopus 로고
    • Bovine serum albumin in aqueous guanidine hydrochloride solutions. Preferential and absolute interactions and comparison with other systems
    • Reisler E, Haik Y, Eisenberg H. 1977. Bovine serum albumin in aqueous guanidine hydrochloride solutions. Preferential and absolute interactions and comparison with other systems. Biochemistry 16:197-203.
    • (1977) Biochemistry , vol.16 , pp. 197-203
    • Reisler, E.1    Haik, Y.2    Eisenberg, H.3
  • 26
    • 33947437221 scopus 로고
    • Physical chemistry of protein solutions. I. Derivation of the equations for the osmotic pressure
    • Scatchard G. 1946. Physical chemistry of protein solutions. I. Derivation of the equations for the osmotic pressure. J Am Chem Soc 68:2315-2319.
    • (1946) J Am Chem Soc , vol.68 , pp. 2315-2319
    • Scatchard, G.1
  • 27
    • 0023068366 scopus 로고
    • The thermodynamic stability of proteins
    • Schellman JA. 1987. The thermodynamic stability of proteins. Annu Rev Biophys Biophys Chem 16:115-137.
    • (1987) Annu Rev Biophys Biophys Chem , vol.16 , pp. 115-137
    • Schellman, J.A.1
  • 28
    • 0025030410 scopus 로고
    • A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures
    • Schellman JA. 1990. A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures. Biophys Chem 37:121-140.
    • (1990) Biophys Chem , vol.37 , pp. 121-140
    • Schellman, J.A.1
  • 29
    • 0027470443 scopus 로고
    • The relation between the free energy of interaction and binding
    • Schellman JA. 1993. The relation between the free energy of interaction and binding. Biophys Chem 45:273-279.
    • (1993) Biophys Chem , vol.45 , pp. 273-279
    • Schellman, J.A.1
  • 30
    • 0002628768 scopus 로고
    • Light scattering in multi-component systems
    • Stockmayer WH. 1950. Light scattering in multi-component systems. J Chem Phys 18:58-61.
    • (1950) J Chem Phys , vol.18 , pp. 58-61
    • Stockmayer, W.H.1
  • 31
    • 0026788012 scopus 로고
    • Water as ligand: Preferential binding and exclusion of denaturants in protein unfolding
    • Timasheff SN. 1992. Water as ligand: Preferential binding and exclusion of denaturants in protein unfolding. Biochemistry 31:9857-9864.
    • (1992) Biochemistry , vol.31 , pp. 9857-9864
    • Timasheff, S.N.1
  • 32
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • Timasheff SN. 1993. The control of protein stability and association by weak interactions with water: How do solvents affect these processes? Annu Rev Biophys Biomol Struct 22:67-97.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 33
    • 0001919558 scopus 로고
    • Preferential interactions of water and co-solvents with proteins
    • Gregory R, ed. New York: Marcel Dekker
    • Timasheff SN. 1994. Preferential interactions of water and co-solvents with proteins. In: Gregory R, ed. Protein-solvent interactions. New York: Marcel Dekker. pp 445-482.
    • (1994) Protein-solvent Interactions , pp. 445-482
    • Timasheff, S.N.1
  • 34
    • 0003102738 scopus 로고
    • The extrapolation of light scattering data to zero concentration
    • Timasheff SN, Kronman MJ. 1959. The extrapolation of light scattering data to zero concentration. Arch Biochem Biophys 83:60-75.
    • (1959) Arch Biochem Biophys , vol.83 , pp. 60-75
    • Timasheff, S.N.1    Kronman, M.J.2
  • 35
    • 0001679156 scopus 로고
    • The effects of neutral salts on the structure and conformational stability of macromolecules in solution
    • Timasheff SN, Fasman GD, eds. New York: Marcel Dekker
    • von Hippel PH, Schleich T. 1969. The effects of neutral salts on the structure and conformational stability of macromolecules in solution. In: Timasheff SN, Fasman GD, eds. Structure and stability of biological macromolecules, vol 2. New York: Marcel Dekker pp 417-574.
    • (1969) Structure and Stability of Biological Macromolecules , vol.2 , pp. 417-574
    • Von Hippel, P.H.1    Schleich, T.2
  • 36
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • Wyman J. 1964. Linked functions and reciprocal effects in hemoglobin: A second look. Adv Protein Chem 19:223-286.
    • (1964) Adv Protein Chem , vol.19 , pp. 223-286
    • Wyman, J.1
  • 37
    • 0031013887 scopus 로고    scopus 로고
    • Mechanism of the stabilization of ribonuclease a by sorbitol: Preferential hydration is greater for the denatured than for the native protein
    • Xie G, Timasheff SN. 1997. Mechanism of the stabilization of ribonuclease A by sorbitol: Preferential hydration is greater for the denatured than for the native protein. Protein Sci 6:211-221.
    • (1997) Protein Sci , vol.6 , pp. 211-221
    • Xie, G.1    Timasheff, S.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.