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Volumn 104, Issue 2, 2003, Pages 489-499

How large are the volume changes accompanying protein transitions and binding?

Author keywords

Conformational changes; Globular proteins; Hydration; Intrinsic packing; Protein binding; Volume

Indexed keywords

PROTEIN; SOLVENT;

EID: 0038487378     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(03)00037-1     Document Type: Article
Times cited : (59)

References (51)
  • 2
    • 0029144073 scopus 로고
    • Hydrostatic and osmotic pressure as tools to study macromolecular recognition
    • Robinson C.R., Sligar S.G. Hydrostatic and osmotic pressure as tools to study macromolecular recognition. Methods Enzymol. 259:1995;395-427.
    • (1995) Methods Enzymol. , vol.259 , pp. 395-427
    • Robinson, C.R.1    Sligar, S.G.2
  • 3
    • 0031714901 scopus 로고    scopus 로고
    • Protein structure and dynamics at high pressure
    • Heremans K., Smeller L. Protein structure and dynamics at high pressure. Biochim. Biophys. Acta. 1386:1998;353-370.
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 353-370
    • Heremans, K.1    Smeller, L.2
  • 4
    • 0035478292 scopus 로고    scopus 로고
    • Pressure provides new insights into protein folding, dynamics and structure
    • Silva J.L., Foguel D., Royer C.A. Pressure provides new insights into protein folding, dynamics and structure. Trends Biochem. Sci. 26:2001;612-618.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 612-618
    • Silva, J.L.1    Foguel, D.2    Royer, C.A.3
  • 5
    • 0017429069 scopus 로고
    • Areas, volumes packing and protein structure
    • Richards F.M. Areas, volumes packing and protein structure. Annu. Rev. Biophys. Bioeng. 6:1977;151-176.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 6
    • 0021195067 scopus 로고
    • Amino acid, peptide and protein volume in solution
    • Zamyatnin A.A. Amino acid, peptide and protein volume in solution. Annu. Rev. Biophys. Bioeng. 13:1984;145-165.
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 145-165
    • Zamyatnin, A.A.1
  • 7
    • 0031790423 scopus 로고    scopus 로고
    • Thermodynamic analysis of biomolecules: A volumetric approach
    • Chalikian T.V., Breslauer K.J. Thermodynamic analysis of biomolecules: a volumetric approach. Curr. Opin. Struct. Biol. 8:1998;657-664.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 657-664
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 8
    • 0030034601 scopus 로고    scopus 로고
    • Compressibility as a means to detect and characterize globular protein states
    • Chalikian T.V., Breslauer K.J. Compressibility as a means to detect and characterize globular protein states. Proc. Natl. Acad. Sci. USA. 93:1996;1012-1014.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1012-1014
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 10
    • 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
  • 11
    • 0021726687 scopus 로고
    • Protein fluctuations and the thermodynamic uncertainty principle
    • Cooper A. Protein fluctuations and the thermodynamic uncertainty principle. Prog. Biophys. Molec. Biol. 44:1984;181-214.
    • (1984) Prog. Biophys. Molec. Biol. , vol.44 , pp. 181-214
    • Cooper, A.1
  • 12
    • 0033934245 scopus 로고    scopus 로고
    • Pressure-induced local unfolding of the Ras binding domain of RalGDS
    • Inoue K., Yamada H., Akasaka K., et al. Pressure-induced local unfolding of the Ras binding domain of RalGDS. Nature Struct. Biol. 7:2000;547-550.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 547-550
    • Inoue, K.1    Yamada, H.2    Akasaka, K.3
  • 13
    • 0035856546 scopus 로고    scopus 로고
    • Two folded conformers of ubiquitin revealed by high-pressure NMR
    • Kitahara R., Yamada R., Akasaka K. Two folded conformers of ubiquitin revealed by high-pressure NMR. Biochemistry. 40:2001;13556-13563.
    • (2001) Biochemistry , vol.40 , pp. 13556-13563
    • Kitahara, R.1    Yamada, R.2    Akasaka, K.3
  • 14
    • 0034602677 scopus 로고    scopus 로고
    • Denaturant-induced movement of the transition state of protein folding revealed by high-pressure stopped-flow measurements
    • Pappenberger G., Saudan C., Becker M., Merbach A.E., Kiefhaber T. Denaturant-induced movement of the transition state of protein folding revealed by high-pressure stopped-flow measurements. Proc. Natl. Acad. Sci. USA. 97:2000;17-22.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 17-22
    • Pappenberger, G.1    Saudan, C.2    Becker, M.3    Merbach, A.E.4    Kiefhaber, T.5
  • 15
    • 0035912726 scopus 로고    scopus 로고
    • Partial molar volume, surface area and hydration changes for equilibrium unfolding and formation of aggregation transition state: High-pressure and cosolute studies on recombinant human IFN-gamma
    • Webb J.N., Webb S.D., Cleland J.L., Carpenter J.F., Randolph T.W. Partial molar volume, surface area and hydration changes for equilibrium unfolding and formation of aggregation transition state: high-pressure and cosolute studies on recombinant human IFN-gamma. Proc. Natl. Acad. Sci. USA. 98:2001;7259-7264.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7259-7264
    • Webb, J.N.1    Webb, S.D.2    Cleland, J.L.3    Carpenter, J.F.4    Randolph, T.W.5
  • 16
    • 0036303731 scopus 로고    scopus 로고
    • Water contributes actively to the rapid crossing of a protein unfolding barrier
    • Jacob M.H., Saudan C., Holtermann G., et al. Water contributes actively to the rapid crossing of a protein unfolding barrier. J. Mol. Biol. 318:2002;837-845.
    • (2002) J. Mol. Biol. , vol.318 , pp. 837-845
    • Jacob, M.H.1    Saudan, C.2    Holtermann, G.3
  • 17
    • 0025855018 scopus 로고
    • Ultrasonic velocimetry of biological compounds
    • Sarvazyan A.P. Ultrasonic velocimetry of biological compounds. Annu. Rev. Biophys. Biophys. Chem. 20:1991;321-342.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 321-342
    • Sarvazyan, A.P.1
  • 18
    • 0027993455 scopus 로고
    • Hydration and partial compressibility of biological compounds
    • Chalikian T.V., Sarvazyan A.P., Breslauer K.J. Hydration and partial compressibility of biological compounds. Biophys. Chem. 51:1994;89-109.
    • (1994) Biophys. Chem. , vol.51 , pp. 89-109
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Breslauer, K.J.3
  • 20
    • 0030298077 scopus 로고    scopus 로고
    • On volume changes accompanying conformational transitions of biopolymers
    • Chalikian T.V., Breslauer K.J. On volume changes accompanying conformational transitions of biopolymers. Biopolymers. 39:1996;619-626.
    • (1996) Biopolymers , vol.39 , pp. 619-626
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 21
    • 0002050426 scopus 로고
    • Conformational transitions of proteins in water and in aqueous mixtures
    • S.N. Timasheff, & G.D. Fasman. New York: Marcel Dekker, Inc
    • Brandts J.F. Conformational transitions of proteins in water and in aqueous mixtures. Timasheff S.N., Fasman G.D. Structure and Stability of Biological Macromolecules. 1969;213-290 Marcel Dekker, Inc, New York.
    • (1969) Structure and Stability of Biological Macromolecules , pp. 213-290
    • Brandts, J.F.1
  • 22
    • 0001529341 scopus 로고    scopus 로고
    • Protein hydration and unfolding-insights from experimental partial specific volumes and unfolded protein models
    • Murphy L.R., Matubayasi N., Payne V.A., Levy R.M. Protein hydration and unfolding-insights from experimental partial specific volumes and unfolded protein models. Fold. Des. 3:1998;105-118.
    • (1998) Fold. Des. , vol.3 , pp. 105-118
    • Murphy, L.R.1    Matubayasi, N.2    Payne, V.A.3    Levy, R.M.4
  • 23
    • 0037171140 scopus 로고    scopus 로고
    • Revisiting volume changes in pressure-induced protein unfolding
    • Royer C.A. Revisiting volume changes in pressure-induced protein unfolding. Biochim. Biophys. Acta. 1595:2002;201-209.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 201-209
    • Royer, C.A.1
  • 24
    • 9444282012 scopus 로고
    • Aqueous solutions of nonpolar gases
    • Pierotti R.A. Aqueous solutions of nonpolar gases. J. Phys. Chem. 69:1965;281-288.
    • (1965) J. Phys. Chem. , vol.69 , pp. 281-288
    • Pierotti, R.A.1
  • 25
    • 33747754400 scopus 로고
    • A scaled particle theory of aqueous and nonaqueous solutions
    • Pierotti R.A. A scaled particle theory of aqueous and nonaqueous solutions. Chem. Rev. 76:1976;717-726.
    • (1976) Chem. Rev. , vol.76 , pp. 717-726
    • Pierotti, R.A.1
  • 26
    • 0001445637 scopus 로고
    • Partial molar volumes of molecules of arbitrary shape and the effect of hydrogen bonding with water
    • Kharakoz D.P. Partial molar volumes of molecules of arbitrary shape and the effect of hydrogen bonding with water. J. Solution Chem. 21:1992;569-595.
    • (1992) J. Solution Chem. , vol.21 , pp. 569-595
    • Kharakoz, D.P.1
  • 27
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly M.J. Solvent-accessible surfaces of proteins and nucleic acids. Science. 221:1983;709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.J.1
  • 28
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • Connolly M.J. Analytical molecular surface calculation. J. Appl. Cryst. 16:1983;548-558.
    • (1983) J. Appl. Cryst. , vol.16 , pp. 548-558
    • Connolly, M.J.1
  • 29
    • 0008047756 scopus 로고    scopus 로고
    • Hydration of globular proteins as derived from the volume and compressibility measurements: Cross correlating thermodynamic and structural data
    • Chalikian T.V., Totrov M., Abagyan R., Breslauer K.J. Hydration of globular proteins as derived from the volume and compressibility measurements: cross correlating thermodynamic and structural data. J. Mol. Biol. 260:1996;588-603.
    • (1996) J. Mol. Biol. , vol.260 , pp. 588-603
    • Chalikian, T.V.1    Totrov, M.2    Abagyan, R.3    Breslauer, K.J.4
  • 30
    • 0000681226 scopus 로고
    • Relation between van der Waals and partial molar volumes of organic molecules in water
    • Edward J.T., Farrell P.G. Relation between van der Waals and partial molar volumes of organic molecules in water. Can. J. Chem. 53:1975;2965-2970.
    • (1975) Can. J. Chem. , vol.53 , pp. 2965-2970
    • Edward, J.T.1    Farrell, P.G.2
  • 32
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • Fink A.L. Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24:1995;495-522.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 495-522
    • Fink, A.L.1
  • 33
    • 0030032461 scopus 로고    scopus 로고
    • The denatured state (the other half of the folding equation) and its role in protein stability
    • Shortle D. The denatured state (the other half of the folding equation) and its role in protein stability. FASEB J. 10:1996;27-34.
    • (1996) FASEB J. , vol.10 , pp. 27-34
    • Shortle, D.1
  • 34
    • 0034581327 scopus 로고    scopus 로고
    • Role of the molten globule state in protein folding
    • Arai M., Kuwajima K. Role of the molten globule state in protein folding. Adv. Protein Chem. 53:2000;209-282.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 209-282
    • Arai, M.1    Kuwajima, K.2
  • 35
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of native-like topology in a denatured protein in 8 M urea
    • Shortle D., Ackerman M.S. Persistence of native-like topology in a denatured protein in 8 M urea. Science. 293:2001;487-489.
    • (2001) Science , vol.293 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 36
    • 18244364614 scopus 로고    scopus 로고
    • Long-range interactions within a nonnative protein
    • Klein-Seetharaman J., Oikawa M., Grimshaw S.B., et al. Long-range interactions within a nonnative protein. Science. 295:2002;1719-1722.
    • (2002) Science , vol.295 , pp. 1719-1722
    • Klein-Seetharaman, J.1    Oikawa, M.2    Grimshaw, S.B.3
  • 38
    • 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
  • 39
    • 0035924822 scopus 로고    scopus 로고
    • Structural thermodynamics of hydration
    • Chalikian T.V. Structural thermodynamics of hydration. J. Phys. Chem. B. 105:2001;12566-12578.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 12566-12578
    • Chalikian, T.V.1
  • 40
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 47:1995;83-229.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 41
    • 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
  • 42
    • 0029011017 scopus 로고
    • Volumetric characterizations of thenative, molten globule and unfolded states of cytochrome c at acidic pH
    • Chalikian T.V., Gindikin V.S., Breslauer K.J. Volumetric characterizations of thenative, molten globule and unfolded states of cytochrome c at acidic pH. J. Mol. Biol. 250:1995;291-306.
    • (1995) J. Mol. Biol. , vol.250 , pp. 291-306
    • Chalikian, T.V.1    Gindikin, V.S.2    Breslauer, K.J.3
  • 43
    • 0030059691 scopus 로고    scopus 로고
    • Spectroscopic and volumetric investigation of cytochrome c unfolding at alkaline pH: Characterization of the base induced unfolded state at 25°C
    • Chalikian T.V., Gindikin V.S., Breslauer K.J. Spectroscopic and volumetric investigation of cytochrome c unfolding at alkaline pH: Characterization of the base induced unfolded state at 25°C. FASEB J. 10:1996;164-170.
    • (1996) FASEB J. , vol.10 , pp. 164-170
    • Chalikian, T.V.1    Gindikin, V.S.2    Breslauer, K.J.3
  • 44
    • 0343247668 scopus 로고    scopus 로고
    • The native and the heat-induced denatured states of α-chymotrypsinogen A: A thermodynamic and spectroscopic study
    • Chalikian T.V., Völker J., Anafi D., Breslauer K.J. The native and the heat-induced denatured states of α-chymotrypsinogen A: A thermodynamic and spectroscopic study. J. Mol. Biol. 274:1997;237-252.
    • (1997) J. Mol. Biol. , vol.274 , pp. 237-252
    • Chalikian, T.V.1    Völker, J.2    Anafi, D.3    Breslauer, K.J.4
  • 45
    • 0034625325 scopus 로고    scopus 로고
    • Volumetric and spectroscopic characterizations of the native and acid-induced denatured states of staphylococcal nuclease
    • Filfil R., Chalikian T.V. Volumetric and spectroscopic characterizations of the native and acid-induced denatured states of staphylococcal nuclease. J. Mol. Biol. 299:2000;829-844.
    • (2000) J. Mol. Biol. , vol.299 , pp. 829-844
    • Filfil, R.1    Chalikian, T.V.2
  • 46
    • 0035824880 scopus 로고    scopus 로고
    • Characterization of pH-induced transitions of β-lactoglobulin: Ultrasonic, densimetric and spectroscopic studies
    • Taulier N., Chalikian T.V. Characterization of pH-induced transitions of β-lactoglobulin: ultrasonic, densimetric and spectroscopic studies. J. Mol. Biol. 314:2001;873-889.
    • (2001) J. Mol. Biol. , vol.314 , pp. 873-889
    • Taulier, N.1    Chalikian, T.V.2
  • 47
    • 0031709390 scopus 로고    scopus 로고
    • Hydration of diglycyl tripeptides with non-polar side chains: A volumetric study
    • Chalikian T.V., Gindikin V.S., Breslauer K.J. Hydration of diglycyl tripeptides with non-polar side chains: a volumetric study. Biophys. Chem. 75:1998;57-71.
    • (1998) Biophys. Chem. , vol.75 , pp. 57-71
    • Chalikian, T.V.1    Gindikin, V.S.2    Breslauer, K.J.3
  • 48
    • 0000493265 scopus 로고    scopus 로고
    • The role of water in protein-ligand interactions: Volumetric characterizations of the binding of 2′-CMP and 3′-CMP to ribonuclease A
    • Dubins D.N., Filfil R. Jr., Macgregor R.B., Chalikian T.V. The role of water in protein-ligand interactions: volumetric characterizations of the binding of 2′-CMP and 3′-CMP to ribonuclease A. J. Phys. Chem. B. 104:2000;390-401.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 390-401
    • Dubins, D.N.1    Filfil R., Jr.2    Macgregor, R.B.3    Chalikian, T.V.4
  • 49
    • 0037470558 scopus 로고    scopus 로고
    • The thermodynamics of protein-protein recognition as characterized by a combination of volumetric and calorimetric techniques: The binding of turkey ovomucoid third domain to α-chymotrypsin
    • R. Filfil, T.V. Chalikian, The thermodynamics of protein-protein recognition as characterized by a combination of volumetric and calorimetric techniques: The binding of turkey ovomucoid third domain to α-chymotrypsin, J. Mol. Biol. (2003) 1271-1288.
    • (2003) J. Mol. Biol. , pp. 1271-1288
    • Filfil, R.1    Chalikian, T.V.2
  • 50
    • 0032841423 scopus 로고    scopus 로고
    • The hydration of nucleic acid duplexes as assessed by a combination of volumetric and structural techniques
    • Chalikian T.V., Völker J., Srinivasan A.R., Olson W.K., Breslauer K.J. The hydration of nucleic acid duplexes as assessed by a combination of volumetric and structural techniques. Biopolymers. 50:1999;459-471.
    • (1999) Biopolymers , vol.50 , pp. 459-471
    • Chalikian, T.V.1    Völker, J.2    Srinivasan, A.R.3    Olson, W.K.4    Breslauer, K.J.5
  • 51
    • 0000137680 scopus 로고    scopus 로고
    • Volumetric properties of nucleic acids
    • Chalikian T.V., Breslauer K.J. Volumetric properties of nucleic acids. Biopolymers. 48:1998;264-280.
    • (1998) Biopolymers , vol.48 , pp. 264-280
    • Chalikian, T.V.1    Breslauer, K.J.2


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