메뉴 건너뛰기




Volumn 101-102, Issue , 2002, Pages 497-511

Generalized derivation of an exact relationship linking different coefficients that characterize thermodynamic effects of preferential interactions

Author keywords

Equilibrium dialysis; Isopiestic distillation; Preferential interactions; Solution thermodynamics; Urea salt interactions; Vapor pressure osmometry

Indexed keywords

LINK PROTEIN; PROTEIN DERIVATIVE; SODIUM CHLORIDE;

EID: 0037059028     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00159-X     Document Type: Article
Times cited : (33)

References (23)
  • 1
    • 0025030410 scopus 로고
    • A simple model for solvation in mixed-solvent. Applications to the stabilization and destabilization of macromolecular structures
    • Schellman J.A. A simple model for solvation in mixed-solvent. Applications to the stabilization and destabilization of macromolecular structures. Biophys. Chem. 37:(1-3):1990;121-140.
    • (1990) Biophys. Chem. , vol.37 , Issue.1-3 , pp. 121-140
    • Schellman, J.A.1
  • 2
    • 77956752195 scopus 로고
    • Thermodynamic analysis of multicomponent solutions
    • Cassassa E.F., Eisenberg H. Thermodynamic analysis of multicomponent solutions. Adv. Protein Chem. 19:1964;287-395.
    • (1964) Adv. Protein Chem. , vol.19 , pp. 287-395
    • Cassassa, E.F.1    Eisenberg, H.2
  • 3
    • 0014201792 scopus 로고
    • Isopiestic compositions as a measure of preferential interactions of macromolecules in two-component solvents. Application to proteins and concentrated aqueous cesium chloride and guanidine hydrochloride
    • Hade E.P.K., Tanford C. Isopiestic compositions as a measure of preferential interactions of macromolecules in two-component solvents. Application to proteins and concentrated aqueous cesium chloride and guanidine hydrochloride. J. Am. Chem. Soc. 89:1967;5034-5044.
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 5034-5044
    • Hade, E.P.K.1    Tanford, C.2
  • 5
    • 0037123063 scopus 로고    scopus 로고
    • Thermodynamic expressions relating different types of preferential interaction coefficients in solutions containing two solute components
    • Anderson C.F., Courtenay E.S., Record M.T. Jr. Thermodynamic expressions relating different types of preferential interaction coefficients in solutions containing two solute components. J. Phys. Chem. B. 106:2002;418-433.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 418-433
    • Anderson, C.F.1    Courtenay, E.S.2    Record M.T., Jr.3
  • 6
    • 0029798239 scopus 로고    scopus 로고
    • Thermodynamic characterization of interactions of native bovine serum albumin with highly excluded (glycine betaine) and moderately accumulated (urea) solutes by a novel application of vapor pressure osmometry
    • Zhang W., Capp M.W., Bond J.P., Anderson C.F., Record M.T. Jr. Thermodynamic characterization of interactions of native bovine serum albumin with highly excluded (glycine betaine) and moderately accumulated (urea) solutes by a novel application of vapor pressure osmometry. Biochemistry. 35:1996;10506-10516.
    • (1996) Biochemistry , vol.35 , pp. 10506-10516
    • Zhang, W.1    Capp, M.W.2    Bond, J.P.3    Anderson, C.F.4    Record M.T., Jr.5
  • 7
    • 0034681955 scopus 로고    scopus 로고
    • Vapor pressure osmometry studies of osmolyte-protein interactions: Implications for the action of osmoprotectants in vivo and for the interpretation of 'osmotic stress' experiments in vitro
    • Courtenay E.S., Capp M.W., Anderson C.F., Record M.T. Jr. Vapor pressure osmometry studies of osmolyte-protein interactions: implications for the action of osmoprotectants in vivo and for the interpretation of 'osmotic stress' experiments in vitro. Biochemistry. 39:2000;4455-4471.
    • (2000) Biochemistry , vol.39 , pp. 4455-4471
    • Courtenay, E.S.1    Capp, M.W.2    Anderson, C.F.3    Record M.T., Jr.4
  • 8
    • 0035176391 scopus 로고    scopus 로고
    • Thermodynamics of interactions of urea and guanidinium salts with protein surface: Relationship between solute effects on protein processes and changes in water-accessible surface area
    • Courtenay E.S., Capp M.W., Record M.T. Jr. Thermodynamics of interactions of urea and guanidinium salts with protein surface: relationship between solute effects on protein processes and changes in water-accessible surface area. Protein Sci. 10:2001;2485-2497.
    • (2001) Protein Sci. , vol.10 , pp. 2485-2497
    • Courtenay, E.S.1    Capp, M.W.2    Record M.T., Jr.3
  • 9
    • 0001918044 scopus 로고
    • Determination of the dominant factors which influence the net hydration of native sodium deoxyribonucleate
    • Hearst J.E. Determination of the dominant factors which influence the net hydration of native sodium deoxyribonucleate. Biopolymers. 3:1965;57-62.
    • (1965) Biopolymers , vol.3 , pp. 57-62
    • Hearst, J.E.1
  • 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. Deoxyribonucleate solutions: sedimentation in a density gradient, partial specific volumes, density and refractive index increments, and preferential interactions. Biopolymers. 6:1968;1077-1100.
    • (1968) Biopolymers , vol.6 , pp. 1077-1100
    • Cohen, G.1    Eisenberg, H.2
  • 11
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • Wyman J. Linked functions and reciprocal effects in hemoglobin: a second look. Adv. Protein Chem. 19:1964;223-286.
    • (1964) Adv. Protein Chem. , vol.19 , pp. 223-286
    • Wyman, J.1
  • 12
    • 0000144150 scopus 로고
    • Salt dependence of oligoion-polyion binding: A thermodynamic description based on preferential interaction coefficients
    • Anderson C.F., Record M.T. Jr. Salt dependence of oligoion-polyion binding: a thermodynamic description based on preferential interaction coefficients. J. Phys. Chem. 97:1993;7116-7126.
    • (1993) J. Phys. Chem. , vol.97 , pp. 7116-7126
    • Anderson, C.F.1    Record M.T., Jr.2
  • 13
    • 0031776135 scopus 로고    scopus 로고
    • Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: A practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts
    • Record M.T. Jr, Zhang W., Anderson C.F. Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts. Adv. Protein Chem. 51:1998;281-353.
    • (1998) Adv. Protein Chem. , vol.51 , pp. 281-353
    • Record M.T., Jr.1    Zhang, W.2    Anderson, C.F.3
  • 14
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff S.N. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 51:1998;355-433.
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-433
    • Timasheff, S.N.1
  • 15
    • 0028076138 scopus 로고
    • Protein and nucleic acid hydration and cosolvent interactions: Establishment of reliable baseline values at high cosolvent concentrations
    • Eisenberg H. Protein and nucleic acid hydration and cosolvent interactions: establishment of reliable baseline values at high cosolvent concentrations. Biophys. Chem. 53:1994;57-68.
    • (1994) Biophys. Chem. , vol.53 , pp. 57-68
    • Eisenberg, H.1
  • 16
    • 0001373502 scopus 로고
    • The thermodynamics of the ternary system: Urea-sodium chloride-water at 25 degrees
    • Bower V.E., Robinson R.A. The thermodynamics of the ternary system: urea-sodium chloride-water at 25 degrees. J. Phys. Chem. 67:1963;1524-1527.
    • (1963) J. Phys. Chem. , vol.67 , pp. 1524-1527
    • Bower, V.E.1    Robinson, R.A.2
  • 17
    • 0027085826 scopus 로고
    • Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols
    • Bhat R., Timasheff S.N. Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols. Protein Sci. 1:1992;1133-1143.
    • (1992) Protein Sci. , vol.1 , pp. 1133-1143
    • Bhat, R.1    Timasheff, S.N.2
  • 18
    • 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., Scholtz J.M. Denaturant m-values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4:1995;2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 19
    • 0033772098 scopus 로고    scopus 로고
    • Thermodynamic analysis of interactions between denaturants and protein surface exposed on unfolding: Interpretation of urea and guanidinium chloride m-values and their correlation with changes in accessible surface area (ASA) using preferential interaction coefficients and the local-bulk domain model, PROTEINS
    • Courtenay E.S., Capp M.W., Saecker R.M., Record M.T. Thermodynamic analysis of interactions between denaturants and protein surface exposed on unfolding: interpretation of urea and guanidinium chloride m-values and their correlation with changes in accessible surface area (ASA) using preferential interaction coefficients and the local-bulk domain model, PROTEINS. Struct. Funct. Genet. 41:(S4):2001;72-85.
    • (2001) Struct. Funct. Genet. , vol.41 , Issue.S4 , pp. 72-85
    • Courtenay, E.S.1    Capp, M.W.2    Saecker, R.M.3    Record, M.T.4
  • 20
    • 0034814860 scopus 로고    scopus 로고
    • Quantitative protein stability measurement in vivo
    • Ghaemmaghami S., Oas T.G. Quantitative protein stability measurement in vivo. Nat. Struct. Biol. 8:2001;879-882.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 879-882
    • Ghaemmaghami, S.1    Oas, T.G.2
  • 21
    • 0001479267 scopus 로고
    • Isotonic solutions. I. The chemical potential of water in aqueous solutions of sodium chloride, potassium chloride, sulfuric acid, sucrose, urea, and glycerol at 25 °C
    • Scatchard G., Hamer W.J., Wood S.E. Isotonic solutions. I. The chemical potential of water in aqueous solutions of sodium chloride, potassium chloride, sulfuric acid, sucrose, urea, and glycerol at 25 °C. J. Am. Chem. Soc. 60:1938;3061-3070.
    • (1938) J. Am. Chem. Soc. , vol.60 , pp. 3061-3070
    • Scatchard, G.1    Hamer, W.J.2    Wood, S.E.3
  • 23
    • 0012083278 scopus 로고
    • Interactions in aqueous solutions. IV. Light scattering of colloidal electrolytes
    • Stigter D. Interactions in aqueous solutions. IV. Light scattering of colloidal electrolytes. J. Phys. Chem. 64:1960;842-846.
    • (1960) J. Phys. Chem. , vol.64 , pp. 842-846
    • Stigter, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.