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Volumn 1749, Issue 2, 2005, Pages 187-213

Stability of proteins: Temperature, pressure and the role of the solvent

Author keywords

Cosolvent and stability; Fluctuation and correlation; Folding denaturing transition; Molecular dynamics simulation; Phase diagram of protein; Protein solvent interaction; Thermodynamics of protein

Indexed keywords

CYTOCHROME C; GLYCEROL; PROTEIN; SOLVENT;

EID: 20144369761     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.03.002     Document Type: Review
Times cited : (159)

References (132)
  • 1
    • 3142624750 scopus 로고    scopus 로고
    • Detecting mad cow disease
    • S.B. Prusiner Detecting mad cow disease Sci. Am. 291 1 2004 60 67
    • (2004) Sci. Am. , vol.291 , Issue.1 , pp. 60-67
    • Prusiner, S.B.1
  • 3
    • 20144368438 scopus 로고    scopus 로고
    • Physik der Proteine
    • G.U. Nienhaus Physik der Proteine Phys.-J. 3 2004 37 43
    • (2004) Phys.-J. , vol.3 , pp. 37-43
    • Nienhaus, G.U.1
  • 5
    • 0032796426 scopus 로고    scopus 로고
    • Role of hydration water in protein unfolding
    • G.W. Robinson, and C.H. Cho Role of hydration water in protein unfolding Biophys. J. 77 1999 3311 3318
    • (1999) Biophys. J. , vol.77 , pp. 3311-3318
    • Robinson, G.W.1    Cho, C.H.2
  • 6
    • 84889802280 scopus 로고    scopus 로고
    • Pressure-temperature phase diagrams of proteins
    • J. Buchner Th. Kiefhaber Wiley-VCH Weinheim
    • W. Doster, and J. Friedrich Pressure-temperature phase diagrams of proteins J. Buchner Th. Kiefhaber Protein Folding Handbook 2004 Wiley-VCH Weinheim 99 126
    • (2004) Protein Folding Handbook , pp. 99-126
    • Doster, W.1    Friedrich, J.2
  • 7
    • 0030932895 scopus 로고    scopus 로고
    • Thermodynamics, molecules and the Gibbs conference
    • J.A. Schellman Thermodynamics, molecules and the Gibbs conference Biophys. Chemist. 64 1997 7 13
    • (1997) Biophys. Chemist. , vol.64 , pp. 7-13
    • Schellman, J.A.1
  • 8
    • 0037920996 scopus 로고    scopus 로고
    • Thermodynamics of protein folding and stability
    • G. Allen JAI Press Inc.
    • A. Cooper Thermodynamics of protein folding and stability G. Allen Proteins: A Comprehensive Treatise vol. 2 1999 JAI Press Inc. 217 270
    • (1999) Proteins: A Comprehensive Treatise , vol.2 , pp. 217-270
    • Cooper, A.1
  • 9
    • 0037438567 scopus 로고    scopus 로고
    • Thermodynamics of protein folding: A microscopic view
    • T. Lazaridis, and M. Karplus Thermodynamics of protein folding: a microscopic view Biophys. Chemist. 100 2003 367 395
    • (2003) Biophys. Chemist. , vol.100 , pp. 367-395
    • Lazaridis, T.1    Karplus, M.2
  • 10
    • 0015236387 scopus 로고
    • Reversible pressure-temperature phase denaturation of chymotrypsinogen
    • S.A. Hawley Reversible pressure-temperature phase denaturation of chymotrypsinogen Biochemistry 10 1971 2436 2442
    • (1971) Biochemistry , vol.10 , pp. 2436-2442
    • Hawley, S.A.1
  • 11
    • 36849117971 scopus 로고
    • Free volume and entropy in condensed systems III. Entropy in binary liquid mixtures; Partial molal entropy in dilute solutions; Structure and thermodynamics in aqueous electrolytes
    • H.S. Frank, and M.W. Evans Free volume and entropy in condensed systems III. Entropy in binary liquid mixtures; partial molal entropy in dilute solutions; structure and thermodynamics in aqueous electrolytes J. Chem. Phys. 13 1945 507 532
    • (1945) J. Chem. Phys. , vol.13 , pp. 507-532
    • Frank, H.S.1    Evans, M.W.2
  • 12
    • 0018588511 scopus 로고
    • Stability of proteins
    • P.L. Privalov Stability of proteins Adv. Protein Chem. 33 1979 167 241
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 13
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • P.L. Privalov, and S.J. Gill Stability of protein structure and hydrophobic interaction Adv. Protein Chem. 39 1988 191 234
    • (1988) Adv. Protein Chem. , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 17
    • 0030028764 scopus 로고    scopus 로고
    • Glycerol decreases the volume and compressibility of protein interior
    • A. Priev, A. Almagor, S. Yedgar, and B. Gavish Glycerol decreases the volume and compressibility of protein interior Biochemistry 35 1996 2061 2066
    • (1996) Biochemistry , vol.35 , pp. 2061-2066
    • Priev, A.1    Almagor, A.2    Yedgar, S.3    Gavish, B.4
  • 18
    • 0026602704 scopus 로고
    • Urea denaturation of barnase: PH dependence and characterization of the unfolded state
    • C.N. Pace, D.V. Laurents, and B.E. Erickson Urea denaturation of barnase: pH dependence and characterization of the unfolded state Biochemistry 31 1992 2728 2734
    • (1992) Biochemistry , vol.31 , pp. 2728-2734
    • Pace, C.N.1    Laurents, D.V.2    Erickson, B.E.3
  • 19
    • 0037137253 scopus 로고    scopus 로고
    • Protein hydration, thermodynamic binding, and preferential hydration
    • S.N. Timasheff Protein hydration, thermodynamic binding, and preferential hydration Biochemistry 41 2002 13473 13482
    • (2002) Biochemistry , vol.41 , pp. 13473-13482
    • Timasheff, S.N.1
  • 20
    • 0037059028 scopus 로고    scopus 로고
    • Generalized derivation of an exact relationship linking different coefficients that characterize thermodynamic effects of preferential interactions
    • C.F. Anderson, D.J. Felitsky, J. Hong, and M.T. Record Generalized derivation of an exact relationship linking different coefficients that characterize thermodynamic effects of preferential interactions Biophys. Chemist. 101-102 2002 497 511
    • (2002) Biophys. Chemist. , vol.101-102 , pp. 497-511
    • Anderson, C.F.1    Felitsky, D.J.2    Hong, J.3    Record, M.T.4
  • 21
    • 0141783830 scopus 로고    scopus 로고
    • Preferential interactions of urea with lysozyme and their linkage to protein denaturation
    • S.N. Timasheff, and G. Xie Preferential interactions of urea with lysozyme and their linkage to protein denaturation Biophys. Chemist. 105 2003 421 448
    • (2003) Biophys. Chemist. , vol.105 , pp. 421-448
    • Timasheff, S.N.1    Xie, G.2
  • 22
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures
    • K. Gekko, and S.N. Timasheff Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures Biochemistry 20 1981 4667 4676
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 23
    • 0019872612 scopus 로고
    • Thermodynamic and kinetic examination of protein stabilization by glycerol
    • K. Gekko, and S.N. Timasheff Thermodynamic and kinetic examination of protein stabilization by glycerol Biochemistry 20 1981 4677 4686
    • (1981) Biochemistry , vol.20 , pp. 4677-4686
    • Gekko, K.1    Timasheff, S.N.2
  • 24
    • 0037162456 scopus 로고    scopus 로고
    • Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components
    • S.N. Timasheff Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components Proc. Natl. Acad. Sci. U. S. A. 99 2002 9721 9726
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 9721-9726
    • Timasheff, S.N.1
  • 25
    • 0346936517 scopus 로고    scopus 로고
    • Proteins in mixed solvents: A molecular-level perspective
    • B.M. Baynes, and B.L. Trout Proteins in mixed solvents: a molecular-level perspective J. Phys. Chem., B 107 2003 14058 14067
    • (2003) J. Phys. Chem., B , vol.107 , pp. 14058-14067
    • Baynes, B.M.1    Trout, B.L.2
  • 26
    • 0032560503 scopus 로고    scopus 로고
    • In disperse solution, "osmotic stress" is a restricted case of preferential interactions
    • S.N. Timasheff In disperse solution, "osmotic stress" is a restricted case of preferential interactions Proc. Natl. Acad. Sci. U. S. A. 95 2002 7363 7367
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7363-7367
    • Timasheff, S.N.1
  • 27
    • 0027231258 scopus 로고
    • On the pH dependence of protein stability
    • A.-S. Yang, and B. Honig On the pH dependence of protein stability J. Mol. Biol. 231 1993 459 474
    • (1993) J. Mol. Biol. , vol.231 , pp. 459-474
    • Yang, A.-S.1    Honig, B.2
  • 28
    • 0014718113 scopus 로고
    • Protein denaturation, Part C
    • C. Tanford Protein denaturation, Part C Adv. Protein Chem. 25 1970 1 95
    • (1970) Adv. Protein Chem. , vol.25 , pp. 1-95
    • Tanford, C.1
  • 29
    • 0842342617 scopus 로고    scopus 로고
    • Estimating hydration changes upon biomolecular reactions from osmotic stress, high pressure, and preferential hydration experiments
    • S. Shimizu Estimating hydration changes upon biomolecular reactions from osmotic stress, high pressure, and preferential hydration experiments Proc. Natl. Acad. Sci. U. S. A. 101 2004 1195 1199
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 1195-1199
    • Shimizu, S.1
  • 30
  • 31
    • 0034635965 scopus 로고    scopus 로고
    • Osmotic stress, crowding, preferential hydration and binding: A comparison of perspectives
    • V.A. Parsegian, R.P. Rand, and D.C. Rau Osmotic stress, crowding, preferential hydration and binding: a comparison of perspectives Proc. Natl. Acad. Sci. U. S. A. 97 2000 3987 3992
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3987-3992
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.C.3
  • 32
    • 0037171151 scopus 로고    scopus 로고
    • Pressure effects on intra- and intermolecular interactions within proteins
    • B.B. Boonyaratanakornkit, C.B. Park, and D.S. Clark Pressure effects on intra- and intermolecular interactions within proteins Biochim. Biophys. Acta 1595 2002 235 249
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 235-249
    • Boonyaratanakornkit, B.B.1    Park, C.B.2    Clark, D.S.3
  • 33
    • 19944392256 scopus 로고    scopus 로고
    • Local compressibilities in insulin as determined from pressure tuning hole burning experiments and MD simulations
    • (in press).
    • C. Schnell, M. Reif, C. Scharnagl, J. Friedrich, Local compressibilities in insulin as determined from pressure tuning hole burning experiments and MD simulations. Phys. Chem. Chem. Phys. (in press).
    • Phys. Chem. Chem. Phys.
    • Schnell, C.1    Reif, M.2    Scharnagl, C.3    Friedrich, J.4
  • 34
    • 0038311869 scopus 로고    scopus 로고
    • Protein stability in mixed solvents: A balance of contact interaction and excluded volume
    • J.A. Schellman Protein stability in mixed solvents: a balance of contact interaction and excluded volume Biophys. J. 85 2003 108 125
    • (2003) Biophys. J. , vol.85 , pp. 108-125
    • Schellman, J.A.1
  • 35
    • 0016292941 scopus 로고
    • Urea and guanidine hydrochlorid denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin
    • R. Green, and C.N. Pace Urea and guanidine hydrochlorid denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin J. Biol. Chem. 249 1974 5388 5393
    • (1974) J. Biol. Chem. , vol.249 , pp. 5388-5393
    • Green, R.1    Pace, C.N.2
  • 38
    • 0037007485 scopus 로고    scopus 로고
    • Fifty years of solvent denaturation
    • J.A. Schellman Fifty years of solvent denaturation Biophys. Chemist. 96 2002 91 101
    • (2002) Biophys. Chemist. , vol.96 , pp. 91-101
    • Schellman, J.A.1
  • 39
    • 84985735713 scopus 로고
    • Excluded volume as a determinant of macromolecular structure and reactivity
    • A.P. Minton Excluded volume as a determinant of macromolecular structure and reactivity Biopolymers 20 1981 2093 2120
    • (1981) Biopolymers , vol.20 , pp. 2093-2120
    • Minton, A.P.1
  • 40
    • 0025608495 scopus 로고
    • The influence of macromolecular crowding on thermodynamic activity: Solubility and dimerization constants for spherical and dumbbell-shaped molecules in a hard-sphere mixture
    • O.G. Berg The influence of macromolecular crowding on thermodynamic activity: solubility and dimerization constants for spherical and dumbbell-shaped molecules in a hard-sphere mixture Biopolymers 30 1990 1027 1037
    • (1990) Biopolymers , vol.30 , pp. 1027-1037
    • Berg, O.G.1
  • 41
    • 0028618410 scopus 로고
    • Contribution of the surface free energy perturbation to protein-solvent interactions
    • Y. Kita, T. Arakawa, T.-Y. Lin, and S. Timasheff Contribution of the surface free energy perturbation to protein-solvent interactions Biochemistry 33 1994 15178 15189
    • (1994) Biochemistry , vol.33 , pp. 15178-15189
    • Kita, Y.1    Arakawa, T.2    Lin, T.-Y.3    Timasheff, S.4
  • 43
    • 0014674115 scopus 로고
    • Extension of the theory of linked functions to incorporate the effects of protein hydration
    • C. Tanford Extension of the theory of linked functions to incorporate the effects of protein hydration J. Mol. Biol. 39 1969 539 544
    • (1969) J. Mol. Biol. , vol.39 , pp. 539-544
    • Tanford, C.1
  • 44
    • 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
    • E.S. Courtenay, M.W. Capp, R.M. Saecker, and M.T. Record 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    Saecker, R.M.3    Record, M.T.4
  • 45
    • 0028962012 scopus 로고
    • Interpretation of preferential interaction coefficients of nonelectrolytes and of electrolyte ions in terms of a 2-domain model
    • M.T. Record, and C.F. Anderson Interpretation of preferential interaction coefficients of nonelectrolytes and of electrolyte ions in terms of a 2-domain model Biophys. J. 68 1995 786 794
    • (1995) Biophys. J. , vol.68 , pp. 786-794
    • Record, M.T.1    Anderson, C.F.2
  • 46
    • 0028862864 scopus 로고
    • The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
    • Y. Liu, and D.W. Bolen The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes Biochemistry 34 1995 12884 12891
    • (1995) Biochemistry , vol.34 , pp. 12884-12891
    • Liu, Y.1    Bolen, D.W.2
  • 47
    • 9744231390 scopus 로고    scopus 로고
    • The Kirkwood-Buff theory and the effect of cosolvents on biochemical reactions
    • S. Shimizu, and C.L. Boon The Kirkwood-Buff theory and the effect of cosolvents on biochemical reactions J. Chem. Phys. 121 2004 9147 9155
    • (2004) J. Chem. Phys. , vol.121 , pp. 9147-9155
    • Shimizu, S.1    Boon, C.L.2
  • 48
    • 10444273367 scopus 로고    scopus 로고
    • Cosolvent interactions with biomolecules: Relating computer simulation data to experimental thermodynamic data
    • P.E. Smith Cosolvent interactions with biomolecules: relating computer simulation data to experimental thermodynamic data J. Phys. Chem., B 108 2004 18716 18724
    • (2004) J. Phys. Chem., B , vol.108 , pp. 18716-18724
    • Smith, P.E.1
  • 49
    • 0037171146 scopus 로고    scopus 로고
    • The effects of osmotic and hydrostatic pressures on macromolecular system
    • J.A. Kornblatt, and M.J. Kornblatt The effects of osmotic and hydrostatic pressures on macromolecular system Biochim. Biophys. Acta 1595 2002 30 47
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 30-47
    • Kornblatt, J.A.1    Kornblatt, M.J.2
  • 50
    • 0037171132 scopus 로고    scopus 로고
    • Pressure-temperature diagrams of biomolecules
    • L. Smeller Pressure-temperature diagrams of biomolecules Biochim. Biophys. Acta 1595 2002 11 29
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 11-29
    • Smeller, L.1
  • 51
    • 0031714901 scopus 로고    scopus 로고
    • Protein structure and dynamics at high pressure
    • K. Heremans, and L. Smeller 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
  • 52
    • 0015820466 scopus 로고
    • Pressure denaturation of metmyoglobin
    • A. Zipp, and W. Kauzmann Pressure denaturation of metmyoglobin Biochemistry 12 1973 4217 4228
    • (1973) Biochemistry , vol.12 , pp. 4217-4228
    • Zipp, A.1    Kauzmann, W.2
  • 55
    • 1642409882 scopus 로고    scopus 로고
    • Effects of chaotropic and kosmotropic cosolvents on the pressure-induced unfolding and denaturation of proteins: An FT-IR study on staphylococcal nuclease
    • H. Herberhold, C.A. Royer, and R. Winter Effects of chaotropic and kosmotropic cosolvents on the pressure-induced unfolding and denaturation of proteins: an FT-IR study on staphylococcal nuclease Biochemistry 43 2004 3336 3345
    • (2004) Biochemistry , vol.43 , pp. 3336-3345
    • Herberhold, H.1    Royer, C.A.2    Winter, R.3
  • 56
    • 0030664959 scopus 로고    scopus 로고
    • Structure of pressure assisted cold denaturated lysozyme and comparison with lysozyme folding intermediates
    • D.P. Nash, and J. Jonas Structure of pressure assisted cold denaturated lysozyme and comparison with lysozyme folding intermediates Biochemistry 36 1997 14375 14383
    • (1997) Biochemistry , vol.36 , pp. 14375-14383
    • Nash, D.P.1    Jonas, J.2
  • 57
    • 0031836878 scopus 로고    scopus 로고
    • High resolution, high pressure NMR-studies of proteins
    • J. Jonas, L. Ballard, and D.P. Nash High resolution, high pressure NMR-studies of proteins Biophys. J. 75 1998 445 452
    • (1998) Biophys. J. , vol.75 , pp. 445-452
    • Jonas, J.1    Ballard, L.2    Nash, D.P.3
  • 59
    • 0031837399 scopus 로고    scopus 로고
    • Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states
    • G.J.A. Vidugiris, and C.A. Royer Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states Biophys. J. 75 1998 463 470
    • (1998) Biophys. J. , vol.75 , pp. 463-470
    • Vidugiris, G.J.A.1    Royer, C.A.2
  • 60
    • 0036195786 scopus 로고    scopus 로고
    • Stability diagram and unfolding of a modified cytochrome c. What happens in the transformation regime?
    • H. Lesch, H. Stadlbauer, J. Friedrich, and J.M. Vanderkooi Stability diagram and unfolding of a modified cytochrome c. What happens in the transformation regime? Biophys. J. 82 2002 1644 1653
    • (2002) Biophys. J. , vol.82 , pp. 1644-1653
    • Lesch, H.1    Stadlbauer, H.2    Friedrich, J.3    Vanderkooi, J.M.4
  • 61
    • 0000503877 scopus 로고
    • Protein hydration from water oxygen-17 magnetic relaxation
    • B. Halle, T. Anderson, S. Forsen, and B. Lindman Protein hydration from water oxygen-17 magnetic relaxation J. Am. Chem. Soc. 103 1981 500 508
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 500-508
    • Halle, B.1    Anderson, T.2    Forsen, S.3    Lindman, B.4
  • 62
    • 0022485951 scopus 로고
    • Determination of water structure around biomolecules using X-ray and neutron diffraction methods
    • H. Savage, and A. Wlodawer Determination of water structure around biomolecules using X-ray and neutron diffraction methods Methods Enzymol. 127 1986 162 183
    • (1986) Methods Enzymol. , vol.127 , pp. 162-183
    • Savage, H.1    Wlodawer, A.2
  • 63
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction
    • J.-S. Jiang, and A.T. Brünger Protein hydration observed by X-ray diffraction J. Mol. Biol. 243 1994 100 115
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.-S.1    Brünger, A.T.2
  • 64
    • 0033546117 scopus 로고    scopus 로고
    • Large-scale networks of hydration water molecules around bovine β-trypsin revealed by cryogenic X-ray crystal structure analysis
    • M. Nakasako Large-scale networks of hydration water molecules around bovine β-trypsin revealed by cryogenic X-ray crystal structure analysis J. Mol. Biol. 289 1999 547 564
    • (1999) J. Mol. Biol. , vol.289 , pp. 547-564
    • Nakasako, M.1
  • 65
    • 0033012840 scopus 로고    scopus 로고
    • Hydration of denatured and molten globule proteins
    • V.P. Denisov, B.H. Jonsson, and B. Halle Hydration of denatured and molten globule proteins Nat. Struct. Biol. 6 1999 253 260
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 253-260
    • Denisov, V.P.1    Jonsson, B.H.2    Halle, B.3
  • 66
    • 0022032982 scopus 로고
    • The stabilization of proteins by osmolytes
    • T. Arakawa, and S.N. Timasheff The stabilization of proteins by osmolytes Biophys. J. 47 1985 411 414
    • (1985) Biophys. J. , vol.47 , pp. 411-414
    • Arakawa, T.1    Timasheff, S.N.2
  • 67
    • 0346488520 scopus 로고
    • The effect of electrostatic polarization of the solvent on electronic absorption spectra in solution
    • N.S. Bayliss The effect of electrostatic polarization of the solvent on electronic absorption spectra in solution J. Chem. Phys. 18 1950 292 296
    • (1950) J. Chem. Phys. , vol.18 , pp. 292-296
    • Bayliss, N.S.1
  • 68
    • 33947550049 scopus 로고
    • Solvent effects in organic spectra: Dipole forces and Franck-Condon principle
    • N.S. Bayliss, and E.G. McRae Solvent effects in organic spectra: dipole forces and Franck-Condon principle J. Phys. Chem. 58 1954 1002 1006
    • (1954) J. Phys. Chem. , vol.58 , pp. 1002-1006
    • Bayliss, N.S.1    McRae, E.G.2
  • 69
    • 0001269334 scopus 로고
    • Dipole moments and polarizabilities of molecules in excited states
    • E.C. Lim Acad. Press New York
    • W. Liptay Dipole moments and polarizabilities of molecules in excited states E.C. Lim Excited States vol. 1 1974 Acad. Press New York 129 229
    • (1974) Excited States , vol.1 , pp. 129-229
    • Liptay, W.1
  • 70
    • 0037653186 scopus 로고    scopus 로고
    • Proteins in electric fields and pressure fields: Basic aspects
    • M. Köhler, J. Friedrich, and J. Fidy Proteins in electric fields and pressure fields: basic aspects Biochim. Biophys. Acta 1386 1998 255 288
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 255-288
    • Köhler, M.1    Friedrich, J.2    Fidy, J.3
  • 71
    • 0032539604 scopus 로고    scopus 로고
    • The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins
    • G. Hummer, S. Garde, A.E. Garcia, M.E. Paulalitis, and L.R. Pratt The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins Proc. Natl. Acad. Sci. U. S. A. 95 1998 1552 1555
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1552-1555
    • Hummer, G.1    Garde, S.2    Garcia, A.E.3    Paulalitis, M.E.4    Pratt, L.R.5
  • 73
    • 20144365303 scopus 로고    scopus 로고
    • Protein phase diagrams: The physics behind their elliptic shape
    • H. Lesch, C. Hecht, and J. Friedrich Protein phase diagrams: the physics behind their elliptic shape J. Chem. Phys. 121 2004 12671 12675
    • (2004) J. Chem. Phys. , vol.121 , pp. 12671-12675
    • Lesch, H.1    Hecht, C.2    Friedrich, J.3
  • 74
    • 0002735565 scopus 로고    scopus 로고
    • Some thermodynamic and kinetic consequences of the phase diagram of protein denaturation
    • K. Heremans Leuven University Press Leuven
    • L. Smeller, and K. Heremans Some thermodynamic and kinetic consequences of the phase diagram of protein denaturation K. Heremans High Pressure Research in Bioscience and Biotechnology 1997 Leuven University Press Leuven 55 58
    • (1997) High Pressure Research in Bioscience and Biotechnology , pp. 55-58
    • Smeller, L.1    Heremans, K.2
  • 75
    • 0002237761 scopus 로고
    • Biomolecules: Where the physics of complexity and simplicity meets
    • H. Frauenfelder, and P.G. Wolynes Biomolecules: where the physics of complexity and simplicity meets Phys. Today 47 2 1994 58 64
    • (1994) Phys. Today , vol.47 , Issue.2 , pp. 58-64
    • Frauenfelder, H.1    Wolynes, P.G.2
  • 77
    • 20144362285 scopus 로고
    • The relation between the changes of thermodynamic quantities at the glass transition and long wavelength fluctuation of glass structure
    • J. Jäckle The relation between the changes of thermodynamic quantities at the glass transition and long wavelength fluctuation of glass structure J. Chem. Phys. 79 1983 4463 4467
    • (1983) J. Chem. Phys. , vol.79 , pp. 4463-4467
    • Jäckle, J.1
  • 78
    • 3943103200 scopus 로고
    • Standard thermodynamics of transfer. Uses and misuses
    • A. Ben-Naim Standard thermodynamics of transfer. Uses and misuses J. Phys. Chem. 82 1978 792 803
    • (1978) J. Phys. Chem. , vol.82 , pp. 792-803
    • Ben-Naim, A.1
  • 79
    • 0031058541 scopus 로고    scopus 로고
    • The statistical-thermodynamics basis for computing of binding affinities: A critical review
    • M.K. Gilson, J.A. Given, B.L. Bush, and J.A. McCammon The statistical-thermodynamics basis for computing of binding affinities: a critical review Biophys. J. 72 1997 1047 1069
    • (1997) Biophys. J. , vol.72 , pp. 1047-1069
    • Gilson, M.K.1    Given, J.A.2    Bush, B.L.3    McCammon, J.A.4
  • 80
    • 0029004611 scopus 로고
    • The volume of atoms on the protein surface calculated from simulation, using Voronoi polyhedra
    • M. Gerstein, J. Tsai, and M. Levitt The volume of atoms on the protein surface calculated from simulation, using Voronoi polyhedra J. Mol. Biol. 249 1995 955 966
    • (1995) J. Mol. Biol. , vol.249 , pp. 955-966
    • Gerstein, M.1    Tsai, J.2    Levitt, M.3
  • 81
    • 0037703765 scopus 로고    scopus 로고
    • Compressibilities of cavities and biological water from Voronoi volumes in hydrated proteins
    • M. Marchi Compressibilities of cavities and biological water from Voronoi volumes in hydrated proteins J. Phys. Chem., B 107 2003 6598 6602
    • (2003) J. Phys. Chem., B , vol.107 , pp. 6598-6602
    • Marchi, M.1
  • 82
    • 0037133342 scopus 로고    scopus 로고
    • Biological water at the protein surface: Dynamical solvation probed directly with femtosecond resolution
    • S.K. Pal, J. Peon, and A.H. Zewail Biological water at the protein surface: dynamical solvation probed directly with femtosecond resolution Proc. Natl. Acad. Sci. U. S. A. 99 2002 1763 1768
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1763-1768
    • Pal, S.K.1    Peon, J.2    Zewail, A.H.3
  • 83
    • 0030325741 scopus 로고    scopus 로고
    • Protein hydration dynamics in aqueous solution
    • V.P. Denison, and B. Halle Protein hydration dynamics in aqueous solution Faraday Discuss. Chem. Soc. 103 1996 227 244
    • (1996) Faraday Discuss. Chem. Soc. , vol.103 , pp. 227-244
    • Denison, V.P.1    Halle, B.2
  • 84
    • 36849122972 scopus 로고
    • High-temperature equation of state by a perturbation method: I. Nonpolar gases
    • R.W. Zwanzig High-temperature equation of state by a perturbation method: I. Nonpolar gases J. Chem. Phys. 22 1954 1320 1426
    • (1954) J. Chem. Phys. , vol.22 , pp. 1320-1426
    • Zwanzig, R.W.1
  • 85
    • 0030573523 scopus 로고    scopus 로고
    • Influence of glycerol on the structure and stability of ferric horse heart myoglobin: A SAXS and circular dichroism study
    • M. Barteri, M.C. Gaudiano, and R. Santucci Influence of glycerol on the structure and stability of ferric horse heart myoglobin: a SAXS and circular dichroism study Biochim. Biophys. Acta 1295 1996 51 58
    • (1996) Biochim. Biophys. Acta , vol.1295 , pp. 51-58
    • Barteri, M.1    Gaudiano, M.C.2    Santucci, R.3
  • 86
    • 0034717156 scopus 로고    scopus 로고
    • Stability and stabilization of globular proteins in solution
    • R. Jaenicke Stability and stabilization of globular proteins in solution J. Biotechnol. 79 2000 193 203
    • (2000) J. Biotechnol. , vol.79 , pp. 193-203
    • Jaenicke, R.1
  • 87
    • 0025856806 scopus 로고
    • Denatured states of proteins
    • K.A. Dill, and D. Shortle Denatured states of proteins Ann. Rev. Biochem. 60 1991 795 825
    • (1991) Ann. Rev. Biochem. , vol.60 , pp. 795-825
    • Dill, K.A.1    Shortle, D.2
  • 88
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • O.B. Ptitsyn 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
  • 89
    • 0030032461 scopus 로고    scopus 로고
    • The denatured state (the other half of the folding equation) and its role in protein stability
    • D. Shortle 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
  • 90
    • 0343580520 scopus 로고    scopus 로고
    • Circular dichroism of denatured barstar suggests residual structure
    • B. Nölting, R. Golbik, A.S. Soler-González, and A.R. Fersht Circular dichroism of denatured barstar suggests residual structure Biochemistry 36 1997 9899 9905
    • (1997) Biochemistry , vol.36 , pp. 9899-9905
    • Nölting, B.1    Golbik, R.2    Soler-González, A.S.3    Fersht, A.R.4
  • 91
    • 0031709523 scopus 로고    scopus 로고
    • Intrinsic protein electric fields: Basic non-covalent interactions and relationship to protein-induced Stark effect
    • M. Laberge Intrinsic protein electric fields: basic non-covalent interactions and relationship to protein-induced Stark effect Biochim. Biophys. Acta 1386 1998 305 330
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 305-330
    • Laberge, M.1
  • 92
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • W. Kauzmann 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
  • 93
    • 0037007468 scopus 로고    scopus 로고
    • Protein stability: The value of 'old literature'
    • F. Franks Protein stability: the value of 'old literature' Biophys. Chemist. 96 2002 117 127
    • (2002) Biophys. Chemist. , vol.96 , pp. 117-127
    • Franks, F.1
  • 94
    • 0037019460 scopus 로고    scopus 로고
    • Molecular dynamics of water at the protein-solvent interface
    • A.R. Bizzari, and S. Cannistraro Molecular dynamics of water at the protein-solvent interface J. Phys. Chem., B 106 2002 6617 6633
    • (2002) J. Phys. Chem., B , vol.106 , pp. 6617-6633
    • Bizzari, A.R.1    Cannistraro, S.2
  • 95
    • 0036286851 scopus 로고    scopus 로고
    • Solvation and hydration of proteins and nucleic acids: A theoretical view of simulation and experiment
    • V. Makarov, B.M. Pettitt, and M. Feig Solvation and hydration of proteins and nucleic acids: a theoretical view of simulation and experiment Acc. Chem. Res. 35 2002 376 384
    • (2002) Acc. Chem. Res. , vol.35 , pp. 376-384
    • Makarov, V.1    Pettitt, B.M.2    Feig, M.3
  • 96
    • 4344602172 scopus 로고    scopus 로고
    • Protein hydration dynamics in solution: A critical survey
    • B. Halle Protein hydration dynamics in solution: a critical survey Philos. Trans. R. Soc. Lond., B 359 2004 1207 1224
    • (2004) Philos. Trans. R. Soc. Lond., B , vol.359 , pp. 1207-1224
    • Halle, B.1
  • 97
    • 2342527858 scopus 로고    scopus 로고
    • Dynamics of water in biological recognition
    • S.K. Pal, and A.H. Zewail Dynamics of water in biological recognition Chem. Res. 104 2004 2099 2123
    • (2004) Chem. Res. , vol.104 , pp. 2099-2123
    • Pal, S.K.1    Zewail, A.H.2
  • 98
    • 0032537184 scopus 로고    scopus 로고
    • Surface topography dependence of biomolecular hydrophobic hydration
    • Y.-K. Cheng, and P.J. Rossky Surface topography dependence of biomolecular hydrophobic hydration Nature 392 1998 696 699
    • (1998) Nature , vol.392 , pp. 696-699
    • Cheng, Y.-K.1    Rossky, P.J.2
  • 99
    • 0036836450 scopus 로고    scopus 로고
    • Protein hydration water: Structure and thermodynamics
    • J.C. Smith, F. Merzel, C. Verma, and S. Fischer Protein hydration water: structure and thermodynamics J. Mol. Liq. 101 2002 27 33
    • (2002) J. Mol. Liq. , vol.101 , pp. 27-33
    • Smith, J.C.1    Merzel, F.2    Verma, C.3    Fischer, S.4
  • 100
    • 0037117502 scopus 로고    scopus 로고
    • Is the first hydration shell of lysozyme of higher density than bulk water?
    • F. Merzel, and J.C. Smith Is the first hydration shell of lysozyme of higher density than bulk water? Proc. Natl. Acad. Sci. U. S. A. 99 2002 5378 5383
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5378-5383
    • Merzel, F.1    Smith, J.C.2
  • 101
    • 0002619244 scopus 로고
    • Effect of high salt concentration in water structure
    • R. Leberman, and A.K. Soper Effect of high salt concentration in water structure Nature 378 1995 364 366
    • (1995) Nature , vol.378 , pp. 364-366
    • Leberman, R.1    Soper, A.K.2
  • 102
    • 0019363328 scopus 로고
    • Effect of protein-solvent interactions on protein conformations
    • G. Némethy, W.J. Peer, and J.A. Scheraga Effect of protein-solvent interactions on protein conformations Annu. Rev. Biophys. Bioeng. 10 1981 459 497
    • (1981) Annu. Rev. Biophys. Bioeng. , vol.10 , pp. 459-497
    • Némethy, G.1    Peer, W.J.2    Scheraga, J.A.3
  • 103
    • 0036252440 scopus 로고    scopus 로고
    • The hydrophobic effect: A new insight from cold denaturation and a two-state water structure
    • C.-J. Tsai, J.V. Maizel Jr., and R. Nussinov The hydrophobic effect: a new insight from cold denaturation and a two-state water structure Crit. Rev. Biochem. Mol. Biol. 37 2002 55 69
    • (2002) Crit. Rev. Biochem. Mol. Biol. , vol.37 , pp. 55-69
    • Tsai, C.-J.1    Maizel Jr., J.V.2    Nussinov, R.3
  • 104
    • 0030696285 scopus 로고    scopus 로고
    • Contribution of water molecules in the interior of a protein to the conformational stability
    • K. Takano, J. Funahashi, Y. Yamagata, S. Fujii, and K. Yutani Contribution of water molecules in the interior of a protein to the conformational stability J. Mol. Biol. 274 1997 132 142
    • (1997) J. Mol. Biol. , vol.274 , pp. 132-142
    • Takano, K.1    Funahashi, J.2    Yamagata, Y.3    Fujii, S.4    Yutani, K.5
  • 105
    • 0033578333 scopus 로고    scopus 로고
    • Binding of buried structural water increases the flexibility of proteins
    • S. Fischer, and C.S. Verma Binding of buried structural water increases the flexibility of proteins Proc. Natl. Acad. Sci. U. S. A. 96 1999 9613 9615
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 9613-9615
    • Fischer, S.1    Verma, C.S.2
  • 106
    • 0024977331 scopus 로고
    • Low-temperature unfolding of a mutant of phage T4 lysozyme: 1. Equilibrium studies
    • B.-L. Chen, and J.A. Schellman Low-temperature unfolding of a mutant of phage T4 lysozyme: 1. Equilibrium studies Biochemistry 28 1989 685 691
    • (1989) Biochemistry , vol.28 , pp. 685-691
    • Chen, B.-L.1    Schellman, J.A.2
  • 107
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • R.L. Baldwin Temperature dependence of the hydrophobic interaction in protein folding Proc. Natl. Acad. Sci. U. S. A. 83 1986 8069 8072
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 8069-8072
    • Baldwin, R.L.1
  • 108
    • 0037446864 scopus 로고    scopus 로고
    • The hydration structure of guanidinium and thiocyanate ions: Implications for protein stability in aqueous solution
    • P.E. Mason, G.W. Neilson, C.E. Dempsey, A.C. Barnes, and J.M. Cruickshank The hydration structure of guanidinium and thiocyanate ions: implications for protein stability in aqueous solution Proc. Natl. Acad. Sci. U. S. A. 100 2003 4557 4561
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4557-4561
    • Mason, P.E.1    Neilson, G.W.2    Dempsey, C.E.3    Barnes, A.C.4    Cruickshank, J.M.5
  • 109
    • 2942555203 scopus 로고    scopus 로고
    • Importance of excluded volume on the solvation of urea in water
    • R.D. Mountain, and D. Thirumalai Importance of excluded volume on the solvation of urea in water J. Phys. Chem., B 108 2004 6826 6831
    • (2004) J. Phys. Chem., B , vol.108 , pp. 6826-6831
    • Mountain, R.D.1    Thirumalai, D.2
  • 110
    • 0038370011 scopus 로고    scopus 로고
    • The molecular basis for chemical denaturation of proteins by urea
    • B.J. Bennion, and V. Daggett The molecular basis for chemical denaturation of proteins by urea Proc. Natl. Acad. Sci. U. S. A. 100 2003 5142 5147
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5142-5147
    • Bennion, B.J.1    Daggett, V.2
  • 111
    • 0038374325 scopus 로고    scopus 로고
    • Why is trehalose an exceptional protein stabilizer?
    • J.K. Kaushik, and R. Bhat Why is trehalose an exceptional protein stabilizer? J. Biol. Chem. 278 2003 26458 26465
    • (2003) J. Biol. Chem. , vol.278 , pp. 26458-26465
    • Kaushik, J.K.1    Bhat, R.2
  • 112
    • 0031195138 scopus 로고    scopus 로고
    • The kosmotropic (structure-forming) effect of compensatory solutes
    • E.A. Galinski, M. Stein, B. Amendt, and M. Kinder The kosmotropic (structure-forming) effect of compensatory solutes Comp. Biochem. Physiol. 117A 1997 357 365
    • (1997) Comp. Biochem. Physiol. , vol.117 , pp. 357-365
    • Galinski, E.A.1    Stein, M.2    Amendt, B.3    Kinder, M.4
  • 113
    • 20144383293 scopus 로고
    • Effect of cosolvent on a tripeptide solution using molecular dynamics simulations
    • N.S. Kang, J.Y. Yu, and M.S. Jhon Effect of cosolvent on a tripeptide solution using molecular dynamics simulations J. Mol. Struct. 355 1995 201 209
    • (1995) J. Mol. Struct. , vol.355 , pp. 201-209
    • Kang, N.S.1    Yu, J.Y.2    Jhon, M.S.3
  • 114
    • 20144380860 scopus 로고    scopus 로고
    • Special issue on: Molecular dynamics simulations of biomolecules
    • Special issue on: Molecular dynamics simulations of biomolecules Acc. Chem. Res. 35 2002
    • (2002) Acc. Chem. Res. , vol.35
  • 117
    • 1942456697 scopus 로고    scopus 로고
    • Recent advances in the development and application of implicit solvent models in biomolecule simulations
    • M. Feig, and C.L. Brooks III Recent advances in the development and application of implicit solvent models in biomolecule simulations Curr. Opin. Struct. Biol. 14 2004 217 224
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 217-224
    • Feig, M.1    Brooks III, C.L.2
  • 118
    • 0033117937 scopus 로고    scopus 로고
    • Investigating protein dynamics in collective coordinate space
    • A. Kitao, and N. Go Investigating protein dynamics in collective coordinate space Curr. Opin. Struct. Biol. 9 1999 164 169
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 164-169
    • Kitao, A.1    Go, N.2
  • 119
    • 0028949547 scopus 로고
    • Theoretical studies of protein folding and unfolding
    • M. Karplus, and A. Sali Theoretical studies of protein folding and unfolding Curr. Opin. Struct. Biol. 5 1995 58 73
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 58-73
    • Karplus, M.1    Sali, A.2
  • 120
    • 0009586942 scopus 로고    scopus 로고
    • Understanding protein folding via free-energy surfaces from theory and experiment
    • A.R. Dinner, A. Sali, L.J. Smith, C.M. Dobson, and M. Karplus Understanding protein folding via free-energy surfaces from theory and experiment TIBS 25 2000 331 339
    • (2000) TIBS , vol.25 , pp. 331-339
    • Dinner, A.R.1    Sali, A.2    Smith, L.J.3    Dobson, C.M.4    Karplus, M.5
  • 122
    • 0037171124 scopus 로고    scopus 로고
    • High pressure simulations of biomolecules
    • E. Paci High pressure simulations of biomolecules Biochim. Biophys. Acta 1595 2002 185 200
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 185-200
    • Paci, E.1
  • 124
    • 0345393320 scopus 로고    scopus 로고
    • Thermodynamics or protein hydration computed by molecular dynamics and normal modes
    • X. Yu, J. Park, and D.M. Leitner Thermodynamics or protein hydration computed by molecular dynamics and normal modes J. Phys. Chem., B 107 2003 12820 12828
    • (2003) J. Phys. Chem., B , vol.107 , pp. 12820-12828
    • Yu, X.1    Park, J.2    Leitner, D.M.3
  • 125
    • 2342614722 scopus 로고    scopus 로고
    • Counteraction of urea-induced protein denaturation by trimethylamine N-oxide
    • B.J. Bennion, and V. Daggett Counteraction of urea-induced protein denaturation by trimethylamine N-oxide Proc. Natl. Acad. Sci. U. S. A. 101 2004 6433 6438
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 6433-6438
    • Bennion, B.J.1    Daggett, V.2
  • 126
    • 0037342275 scopus 로고    scopus 로고
    • Protein structure and dynamics in nonaqueous solvents: Insight from molecular dynamics studies
    • C.M. Soares, V.H. Teixeira, and A.M. Baptista Protein structure and dynamics in nonaqueous solvents: insight from molecular dynamics studies Biophys. J. 84 2003 1628 1641
    • (2003) Biophys. J. , vol.84 , pp. 1628-1641
    • Soares, C.M.1    Teixeira, V.H.2    Baptista, A.M.3
  • 127
    • 0035144443 scopus 로고    scopus 로고
    • Molecular dynamics simulations of carboxy-myoglobin embedded in a trehalose-water matrix
    • G. Cottone, L. Cordone, and G. Ciccotti Molecular dynamics simulations of carboxy-myoglobin embedded in a trehalose-water matrix Biophys. J. 80 2001 931 938
    • (2001) Biophys. J. , vol.80 , pp. 931-938
    • Cottone, G.1    Cordone, L.2    Ciccotti, G.3
  • 128
    • 0037339403 scopus 로고    scopus 로고
    • Selective excitation of native fluctuations during thermal unfolding simulations: Horse heart cytochrome c as a case study
    • D. Roccatano, I. Daidone, M.-A. Ceruso, C. Bossa, and A. Di Nola Selective excitation of native fluctuations during thermal unfolding simulations: horse heart cytochrome c as a case study Biophys. J. 84 2003 1876 1883
    • (2003) Biophys. J. , vol.84 , pp. 1876-1883
    • Roccatano, D.1    Daidone, I.2    Ceruso, M.-A.3    Bossa, C.4    Di Nola, A.5
  • 129
    • 0347949633 scopus 로고    scopus 로고
    • Molecular probes: What is the range of their interaction with the environment?
    • H. Lesch, J. Schlichter, J. Friedrich, and J.M. Vanderkooi Molecular probes: what is the range of their interaction with the environment? Biophys. J. 86 2004 467 472
    • (2004) Biophys. J. , vol.86 , pp. 467-472
    • Lesch, H.1    Schlichter, J.2    Friedrich, J.3    Vanderkooi, J.M.4
  • 130
    • 23244434654 scopus 로고    scopus 로고
    • Local compressibilities of proteins: Comparison of optical experiments and simulations for horse heart cytochrome c
    • (in press).
    • C. Scharnagl, M. Reif, J. Friedrich, Local compressibilities of proteins: comparison of optical experiments and simulations for horse heart cytochrome c, Biophys. J. (in press).
    • Biophys. J.
    • Scharnagl, C.1    Reif, M.2    Friedrich, J.3
  • 132
    • 0036220998 scopus 로고    scopus 로고
    • The enzyme horseradish peroxidase is less compressible at higher pressure
    • L. Smeller, and J. Fidy The enzyme horseradish peroxidase is less compressible at higher pressure Biophys. J. 82 2002 426 436
    • (2002) Biophys. J. , vol.82 , pp. 426-436
    • Smeller, L.1    Fidy, J.2


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