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Volumn 72, Issue 3, 1997, Pages 1022-1030

Probing protein hydration and conformational states in solution

Author keywords

[No Author keywords available]

Indexed keywords

HEXOKINASE; MACROGOL; WATER;

EID: 0031048189     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78754-X     Document Type: Article
Times cited : (85)

References (35)
  • 1
    • 0000539364 scopus 로고
    • Glucose-induced conformational change in yeast hexokinase
    • Bennett, W. S. J., and T. A. Steitz. 1978. Glucose-induced conformational change in yeast hexokinase. Proc. Natl. Acad. Sci. USA. 75:4848-4852.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4848-4852
    • Bennett, W.S.J.1    Steitz, T.A.2
  • 2
    • 0019201173 scopus 로고
    • Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer
    • Bennett, W. S. J., and T. A. Steitz. 1980. Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer. J. Mol. Biol. 140:211-230.
    • (1980) J. Mol. Biol. , vol.140 , pp. 211-230
    • Bennett, W.S.J.1    Steitz, T.A.2
  • 4
    • 0027400112 scopus 로고
    • Probing alamethicin channels with water-soluble polymers: Effect on conductance of channel states
    • Bezrukov, S. M., and I. Vodyanoy. 1993. Probing alamethicin channels with water-soluble polymers: effect on conductance of channel states. Biophys. J. 64:16-25.
    • (1993) Biophys. J. , vol.64 , pp. 16-25
    • Bezrukov, S.M.1    Vodyanoy, I.2
  • 5
    • 0027085826 scopus 로고
    • Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols
    • Bhat, R., and S. N. Timasheff. 1992. Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols. Protein Sci. 1:1133-1143.
    • (1992) Protein Sci. , vol.1 , pp. 1133-1143
    • Bhat, R.1    Timasheff, S.N.2
  • 6
    • 0026535070 scopus 로고
    • Protein solvation in allosteric regulation: A water effect on hemoglobin
    • Colombo, M. F., D. C. Rau, and V. A. Parsegian. 1992. Protein solvation in allosteric regulation: a water effect on hemoglobin. Science. 256: 655-659.
    • (1992) Science , vol.256 , pp. 655-659
    • Colombo, M.F.1    Rau, D.C.2    Parsegian, V.A.3
  • 7
    • 0027819337 scopus 로고
    • Hypersensitivity of an enzyme reaction to solvent water
    • Dzingeleski, G. D., and R. Wolfenden. 1993. Hypersensitivity of an enzyme reaction to solvent water. Biochemistry. 32:9143-9147.
    • (1993) Biochemistry , vol.32 , pp. 9143-9147
    • Dzingeleski, G.D.1    Wolfenden, R.2
  • 8
    • 0027018324 scopus 로고
    • New expressions to describe solution nonideal osmotic pressure, freezing point depression, and vapor pressure
    • Fullerton, G. D., R. J. Zimmerman, C. I. Cantu, and I. L. Cameron. 1992. New expressions to describe solution nonideal osmotic pressure, freezing point depression, and vapor pressure. Biochem. Cell. Biol. 70: 1325-1331.
    • (1992) Biochem. Cell. Biol. , vol.70 , pp. 1325-1331
    • Fullerton, G.D.1    Zimmerman, R.J.2    Cantu, C.I.3    Cameron, I.L.4
  • 9
    • 0028961741 scopus 로고
    • Water release associated with specific binding of gal repressor
    • Garner, M. M., and D. C. Rau. 1995. Water release associated with specific binding of gal repressor. EMBO J. 14:1257-1263.
    • (1995) EMBO J. , vol.14 , pp. 1257-1263
    • Garner, M.M.1    Rau, D.C.2
  • 10
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M., A. M. Lesk, and C. Chothia. 1994. Structural mechanisms for domain movements in proteins. Biochemistry. 33:6739-6749.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 11
    • 0343852100 scopus 로고
    • Oliver and Boyd, Edinburgh and London
    • Haldane, J. S. 1928. Osmosis in Liquids. Oliver and Boyd, Edinburgh and London.
    • (1928) Osmosis in Liquids
    • Haldane, J.S.1
  • 12
    • 0017152977 scopus 로고
    • Yeast hexokinase: Substrate-induced association-dissociation reactions in the binding of glucose to hexokinase P-II
    • Hoggett, J. G., and G. L. Kellett. 1976. Yeast hexokinase: substrate-induced association-dissociation reactions in the binding of glucose to hexokinase P-II. Enr. J. Biochem. 66:65-77.
    • (1976) Enr. J. Biochem. , vol.66 , pp. 65-77
    • Hoggett, J.G.1    Kellett, G.L.2
  • 14
    • 0025185780 scopus 로고
    • A nontraditional role for water in the cytochrome c oxidase reaction
    • Kornblatt, J. A., and G. H. Bon Hoa. 1990. A nontraditional role for water in the cytochrome c oxidase reaction. Biochemistry. 29:9370-9376.
    • (1990) Biochemistry , vol.29 , pp. 9370-9376
    • Kornblatt, J.A.1    Bon Hoa, G.H.2
  • 15
    • 77956904566 scopus 로고
    • The molecular basis for enzyme regulation
    • P. D. Boyer, editor. Academic Press, New York
    • Koshland, D. E. (1970). The molecular basis for enzyme regulation. In The Enzymes, Vol. 1, P. D. Boyer, editor. Academic Press, New York. 341-396.
    • (1970) The Enzymes , vol.1 , pp. 341-396
    • Koshland, D.E.1
  • 17
    • 0019873587 scopus 로고
    • Interaction of calf brain tubulin with glycerol
    • Na, G. C., and S. N. Timasheff. 1981. Interaction of calf brain tubulin with glycerol. J. Mol. Biol. 151:165-178.
    • (1981) J. Mol. Biol. , vol.151 , pp. 165-178
    • Na, G.C.1    Timasheff, S.N.2
  • 18
    • 0022459444 scopus 로고
    • Osmotic stress for the direct measurement of intermolecular forces
    • Parsegian, V. A., R. P. Rand, N. L. Fuller, and D. C. Rau. 1986. Osmotic stress for the direct measurement of intermolecular forces. Methods Enzymol. 127:400-416.
    • (1986) Methods Enzymol. , vol.127 , pp. 400-416
    • Parsegian, V.A.1    Rand, R.P.2    Fuller, N.L.3    Rau, D.C.4
  • 19
    • 0029130871 scopus 로고
    • Macromolecules and water: Probing with osmotic stress
    • Parsegian, V. A., R. P. Rand, and D. C. Rau. 1995. Macromolecules and water: probing with osmotic stress. Methods Enzymol. 259:43-94.
    • (1995) Methods Enzymol. , vol.259 , pp. 43-94
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.C.3
  • 20
    • 0027155787 scopus 로고
    • Measured changes in protein solvation with substrate binding and turnover
    • Rand, R. P., N. L. Fuller, P. Butko, G. Francis, and P. Nicholls. 1993. Measured changes in protein solvation with substrate binding and turnover. Biochemistry. 32:5925-5929.
    • (1993) Biochemistry , vol.32 , pp. 5925-5929
    • Rand, R.P.1    Fuller, N.L.2    Butko, P.3    Francis, G.4    Nicholls, P.5
  • 21
    • 0024378918 scopus 로고
    • Hydration forces between phospholipid bilayers
    • Rand, R. P., and V. A. Parsegian. 1989. Hydration forces between phospholipid bilayers. Biochim. Biophys. Acta. 988:351-376.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 351-376
    • Rand, R.P.1    Parsegian, V.A.2
  • 22
    • 0001533502 scopus 로고
    • Measurement of the repulsive force between polyelectrolyte molecules in ionic solution: Hydration forces between parallel helices
    • Rau, D. C., B. Lee, and V. A. Parsegian. 1984. Measurement of the repulsive force between polyelectrolyte molecules in ionic solution: hydration forces between parallel helices. Proc. Natl. Acad. Sci. USA. 81:2621-2625.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2621-2625
    • Rau, D.C.1    Lee, B.2    Parsegian, V.A.3
  • 23
    • 0025707003 scopus 로고
    • Direct measurement of forces between linear polysaccharides xanthan and schizophyllan
    • Rau, D. C., and V. A. Parsegian. 1990. Direct measurement of forces between linear polysaccharides xanthan and schizophyllan. Science. 249:1278-1281.
    • (1990) Science , vol.249 , pp. 1278-1281
    • Rau, D.C.1    Parsegian, V.A.2
  • 24
    • 0026597099 scopus 로고
    • Voltage-sensitive and solvent-sensitive processes in ion channel gating
    • Rayner, M. D., J. G. Starkus, P. C. Ruben, and D. A. Alicata. 1992. Voltage-sensitive and solvent-sensitive processes in ion channel gating. Biophys. J. 61:96-108.
    • (1992) Biophys. J. , vol.61 , pp. 96-108
    • Rayner, M.D.1    Starkus, J.G.2    Ruben, P.C.3    Alicata, D.A.4
  • 25
    • 0028962012 scopus 로고
    • Interpretation of preferential interaction coefficients of nonelectrolyte and electrolyte ions in terms of a two-domain model
    • Record, M. T. J., and C. F. Anderson. 1995. Interpretation of preferential interaction coefficients of nonelectrolyte and electrolyte ions in terms of a two-domain model. Biophys. J. 68:786-794.
    • (1995) Biophys. J. , vol.68 , pp. 786-794
    • Record, M.T.J.1    Anderson, C.F.2
  • 27
    • 0029144073 scopus 로고
    • Hydrostatic and osmotic pressure as tools to study macromolecular recognition
    • Robinson, C. R., and S. G. Sugar. 1995. Hydrostatic and osmotic pressure as tools to study macromolecular recognition. Methods Enzymol. 259: 395-426.
    • (1995) Methods Enzymol. , vol.259 , pp. 395-426
    • Robinson, C.R.1    Sugar, S.G.2
  • 28
    • 0028931707 scopus 로고
    • The osmotic sensitivity of netropsin analogue binding to DNA
    • Sidorova, N. Y., and D. C. Rau. 1995. The osmotic sensitivity of netropsin analogue binding to DNA. Biopolymers. 35:377-384.
    • (1995) Biopolymers , vol.35 , pp. 377-384
    • Sidorova, N.Y.1    Rau, D.C.2
  • 29
    • 0026788012 scopus 로고
    • Water as ligand: Preferential binding and exclusion of denaturants in protein unfolding
    • Timasheff, S. N. 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
  • 30
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • Timasheff, S. N. 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
  • 31
    • 0020484780 scopus 로고
    • Substrate synergism and the kinetic mechanism of yeast hexokinase
    • Viola, R. E., F. M. Raushel, A. R. Rendina, and W. W. Cleland. 1982. Substrate synergism and the kinetic mechanism of yeast hexokinase. Biochemistry. 21:1295-1302.
    • (1982) Biochemistry , vol.21 , pp. 1295-1302
    • Viola, R.E.1    Raushel, F.M.2    Rendina, A.R.3    Cleland, W.W.4
  • 32
    • 0027517413 scopus 로고
    • Probing alamethicin channels with water-soluble polymers: Size-modulated osmotic action
    • Vodyanoy, I., S. M. Bezrukov, and V. A. Parsegian. 1993. Probing alamethicin channels with water-soluble polymers: size-modulated osmotic action. Biophys. J. 65:2097-2105.
    • (1993) Biophys. J. , vol.65 , pp. 2097-2105
    • Vodyanoy, I.1    Bezrukov, S.M.2    Parsegian, V.A.3
  • 33
    • 0024283362 scopus 로고
    • Synergistic binding of glucose and aluminum*ATP to hexokinase from Saccharomyces cerevisiae
    • Woolfitt, A. R., G. L. Kellett, and J. G. Hoggett. 1988. Synergistic binding of glucose and aluminum*ATP to hexokinase from Saccharomyces cerevisiae. Biochim. Biophys. Acta. 955:346-351.
    • (1988) Biochim. Biophys. Acta , vol.955 , pp. 346-351
    • Woolfitt, A.R.1    Kellett, G.L.2    Hoggett, J.G.3
  • 34
    • 0023041574 scopus 로고
    • Polymer inaccessible volume changes during opening and closing of a voltage-dependent ionic channel
    • Zimmerberg, J., and V. A. Parsegian. 1986. Polymer inaccessible volume changes during opening and closing of a voltage-dependent ionic channel. Nature. 323:36-39.
    • (1986) Nature , vol.323 , pp. 36-39
    • Zimmerberg, J.1    Parsegian, V.A.2
  • 35
    • 0027318513 scopus 로고
    • Molecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmerman, S. B., and A. P. Minton. 1993. Molecular crowding: biochemical, biophysical, and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 22:27-65.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2


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