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Volumn 185, Issue , 2014, Pages 19-24

Thermodynamic analysis of osmolyte effect on thermal stability of ribonuclease A in terms of water activity

Author keywords

Free energy for protein unfolding; m Value; Osmolyte; RNase; Thermal unfolding of protein; Water activity

Indexed keywords

PROTEIN; RIBONUCLEASE A; WATER;

EID: 84888334720     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2013.10.004     Document Type: Article
Times cited : (28)

References (52)
  • 2
    • 24644450812 scopus 로고    scopus 로고
    • Organic osmolytes as compatible, metabolic and counteracting cytoprotectants in high osmolarity and other stresses
    • DOI 10.1242/jeb.01730
    • P.H. Yancey Organic osmolytes as compatible, metabolic and counteracting cytoprotectants in high osmolarity and other stresses J. Exp. Biol. 208 2005 2819 2830 (Pubitemid 41265173)
    • (2005) Journal of Experimental Biology , vol.208 , Issue.15 , pp. 2819-2830
    • Yancey, P.H.1
  • 3
    • 0026631716 scopus 로고
    • Increased thermal stability of proteins in the presence of naturally occurring osmolytes
    • M.M. Santoro, Y. Liu, S.M.A. Khan, L.X. Hou, and D.W. Bolen Increased thermal stability of proteins in the presence of naturally occurring osmolytes Biochemistry 31 1992 5278 5283
    • (1992) Biochemistry , vol.31 , pp. 5278-5283
    • Santoro, M.M.1    Liu, Y.2    Khan, S.M.A.3    Hou, L.X.4    Bolen, D.W.5
  • 4
    • 4344614677 scopus 로고    scopus 로고
    • Effects of naturally occurring osmolytes on protein stability and solubility: Issues important in protein crystallization
    • DOI 10.1016/j.ymeth.2004.03.022, PII S1046202304001136
    • D.W. Bolen Effects of naturally occurring osmolytes on protein stability and solubility: issues important in protein crystallization Methods 34 2004 312 322 (Pubitemid 39119815)
    • (2004) Methods , vol.34 , Issue.3 , pp. 312-322
    • Bolen, D.W.1
  • 5
    • 27744555656 scopus 로고    scopus 로고
    • Protein folding, stability, and solvation structure in osmolyte solutions
    • DOI 10.1529/biophysj.105.067330
    • J. Rösgen, B.M. Pettitt, and D.W. Bolen Protein folding, stability, and solvation structure in osmolyte solutions Biophys. J. 89 2005 2988 2997 (Pubitemid 41636055)
    • (2005) Biophysical Journal , vol.89 , Issue.5 , pp. 2988-2997
    • Rosgen, J.1    Pettitt, B.M.2    Bolen, D.W.3
  • 6
    • 33645296824 scopus 로고    scopus 로고
    • Osmolyte-induced protein folding free energy changes
    • P. Wu, and D.W. Bolen Osmolyte-induced protein folding free energy changes Struct. Funct. Bioinformatics 63 2006 290 296
    • (2006) Struct. Funct. Bioinformatics , vol.63 , pp. 290-296
    • Wu, P.1    Bolen, D.W.2
  • 7
    • 33746882148 scopus 로고    scopus 로고
    • Metrics that Differentiate the Origins of Osmolyte Effects on Protein Stability: A Test of the Surface Tension Proposal
    • DOI 10.1016/j.jmb.2006.07.003, PII S0022283606008564
    • M. Auton, A.C.M. Ferreon, and D.W. Bolen Metrics that differentiate the origins of osmolyte effects on protein stability: a test of the surface tension proposal J. Mol. Biol. 361 2006 983 992 (Pubitemid 44192588)
    • (2006) Journal of Molecular Biology , vol.361 , Issue.5 , pp. 983-992
    • Auton, M.1    Ferreon, A.C.M.2    Bolen, D.W.3
  • 9
    • 33846521172 scopus 로고    scopus 로고
    • Mixed osmolytes: The degree to which one osmolyte affects the protein stabilizing ability of another
    • DOI 10.1110/ps.062610407
    • L.M.F. Holthauzen, and D.W. Bolen Mixed osmolytes: the degree to which one osmolyte affects the protein stabilizing ability of another Protein Sci. 16 2007 293 298 (Pubitemid 46155777)
    • (2007) Protein Science , vol.16 , Issue.2 , pp. 293-298
    • Holthauzen, L.M.F.1    Bolen, D.W.2
  • 10
    • 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
  • 11
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • J. Wyman 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
    • 0026788012 scopus 로고
    • Water as ligand: Preferential binding and exclusion of denaturants in protein unfolding
    • S.N. Timasheff Water as ligand: preferential binding and exclusion of denaturants in protein unfolding Biochemistry 31 1992 9857 9864
    • (1992) Biochemistry , vol.31 , pp. 9857-9864
    • Timasheff, S.N.1
  • 13
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • S.N. Timasheff The control of protein stability and association by weak interactions with water: how do solvents affect these processes Annu. Rev. Biophys. Biomol. Struct. 22 1993 67 97 (Pubitemid 23180317)
    • (1993) Annual Review of Biophysics and Biomolecular Structure , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 15
    • 33645067608 scopus 로고
    • Inversion of the Kirkwood-Buff theory of solutions: Application to the water-ethanol system
    • A. Ben-Naim Inversion of the Kirkwood-Buff theory of solutions: application to the water-ethanol system J. Chem. Phys. 67 1977 4884 4890
    • (1977) J. Chem. Phys. , vol.67 , pp. 4884-4890
    • Ben-Naim, A.1
  • 16
    • 0037075401 scopus 로고    scopus 로고
    • Molecular association in solution: A Kirkwood-Buff analysis of sodium chloride, ammonium sulfate, guanidinium chloride, urea, and 2,2,2- trifluoroethanol in water
    • DOI 10.1021/jp011462h
    • R. Chitra, and P.E. Smith Molecular association in solution: a Kirkwood-Buff analysis of sodium chloride, ammonium sulfate, guanidinium chloride, urea, and 2,2,2-trifluoroethanol in water J. Phys. Chem. B 106 2002 1491 1500 (Pubitemid 35276118)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.6 , pp. 1491-1500
    • Chitra, R.1    Smith, P.E.2
  • 17
    • 0842342617 scopus 로고    scopus 로고
    • Estimating hydration changes upon biomolecular reactions from osmotic stress, high pressure, and preferential hydration experiments
    • DOI 10.1073/pnas.0305836101
    • S. Shimizu Estimating hydration changes upon biomolecular reactions from osmotic stress, high pressure, and preferential hydration experiments PNAS 101 2004 1195 1199 (Pubitemid 38182665)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.5 , pp. 1195-1199
    • Shimizu, S.1
  • 18
    • 1842426176 scopus 로고    scopus 로고
    • Estimation of excess solvation numbers of water and cosolvents from preferential interaction and volumetric experiments
    • S. Shimizu Estimation of excess solvation numbers of water and cosolvents from preferential interaction and volumetric experiments J. Chem. Phys. 120 2004 4989 4990
    • (2004) J. Chem. Phys. , vol.120 , pp. 4989-4990
    • Shimizu, S.1
  • 19
    • 3242690040 scopus 로고    scopus 로고
    • Preferential hydration and the exclusion of cosolvents from protein surfaces
    • S. Shimizu, and D.J. Smith Preferential hydration and the exclusion of cosolvents from protein surfaces J. Chem. Phys. 121 2004 1148 1154
    • (2004) J. Chem. Phys. , vol.121 , pp. 1148-1154
    • Shimizu, S.1    Smith, D.J.2
  • 20
    • 33644678401 scopus 로고    scopus 로고
    • Preferential hydration of proteins: A Kirkwood-Buff approach
    • DOI 10.1016/j.cplett.2006.01.034, PII S0009261406000820
    • S. Shimizu, and N. Matsubayashi Preferential hydration of proteins: a Kirkwood-Buff approach Chem. Phys. Lett. 420 2006 518 522 (Pubitemid 43332880)
    • (2006) Chemical Physics Letters , vol.420 , Issue.4-6 , pp. 518-522
    • Shimizu, S.1    Matubayasi, N.2
  • 21
    • 80052923011 scopus 로고    scopus 로고
    • Molecular origin of the cosolvent-induced changes in the thermal stability of proteins
    • S. Shimizu Molecular origin of the cosolvent-induced changes in the thermal stability of proteins Chem. Phys. Lett. 514 2011 156 158
    • (2011) Chem. Phys. Lett. , vol.514 , pp. 156-158
    • Shimizu, S.1
  • 22
    • 33947730947 scopus 로고    scopus 로고
    • An analysis of the molecular origin of osmolyte-dependent protein stability
    • DOI 10.1110/ps.062671607
    • J. Rösgen, B.M. Pettiitt, and D.W. Bolen An analysis of the molecular origin of osmolyte-dependent protein stability Protein Sci. 16 2007 733 743 (Pubitemid 46507002)
    • (2007) Protein Science , vol.16 , Issue.4 , pp. 733-743
    • Rosgen, J.1    Pettitt, B.M.2    Bolen, D.W.3
  • 23
    • 57049105810 scopus 로고    scopus 로고
    • Structural thermodynamics of protein preferential solvation: Osmolyte solvation of proteins, amino acids, and peptides
    • M. Auton, D.W. Bolen, and J. Rösgen Structural thermodynamics of protein preferential solvation: osmolyte solvation of proteins, amino acids, and peptides Proteins 73 2008 802 813
    • (2008) Proteins , vol.73 , pp. 802-813
    • Auton, M.1    Bolen, D.W.2    Rösgen, J.3
  • 24
    • 0026535070 scopus 로고
    • Protein salvation in allosteric regulation: A water effect on hemoglobin
    • M.F. Colombo, D.C. Rau, and V.A. Parsegian Protein salvation in allosteric regulation: a water effect on hemoglobin Science 256 1992 655 659
    • (1992) Science , vol.256 , pp. 655-659
    • Colombo, M.F.1    Rau, D.C.2    Parsegian, V.A.3
  • 26
    • 0031892702 scopus 로고    scopus 로고
    • Three solutions of the protein solubility problem
    • W.T. Jenkins Three solutions of the protein solubility problem Protein Sci. 7 1998 376 382 (Pubitemid 28092859)
    • (1998) Protein Science , vol.7 , Issue.2 , pp. 376-382
    • Jenkins, W.T.1
  • 27
    • 34250822854 scopus 로고    scopus 로고
    • Hydration state change of proteins upon unfolding in sugar solutions
    • DOI 10.1016/j.bbapap.2007.05.008, PII S1570963907001161
    • O. Miyawaki Hydration state change of proteins upon unfolding in sugar solutions Biochim. Biophys. Acta 1774 2007 928 935 (Pubitemid 46977844)
    • (2007) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1774 , Issue.7 , pp. 928-935
    • Miyawaki, O.1
  • 28
    • 67849118608 scopus 로고    scopus 로고
    • Thermodynamic analysis of protein unfolding in aqueous solutions as a multisite reaction of protein with water and solute molecules
    • O. Miyawaki Thermodynamic analysis of protein unfolding in aqueous solutions as a multisite reaction of protein with water and solute molecules Biophys. Chem. 144 2009 46 52
    • (2009) Biophys. Chem. , vol.144 , pp. 46-52
    • Miyawaki, O.1
  • 29
    • 78951478529 scopus 로고    scopus 로고
    • Thermodynamic analysis of alcohol effect on thermal stability of proteins
    • O. Miyawaki, and M. Tatsuno Thermodynamic analysis of alcohol effect on thermal stability of proteins J. Biosci. Bioeng. 111 2011 198 203
    • (2011) J. Biosci. Bioeng. , vol.111 , pp. 198-203
    • Miyawaki, O.1    Tatsuno, M.2
  • 30
    • 36849096669 scopus 로고
    • Solute-solute interactions in aqueous solutions
    • J.J. Kozak, W.S. Knight, and W. Kauzmann Solute-solute interactions in aqueous solutions J. Chem. Phys. 48 1968 675 690
    • (1968) J. Chem. Phys. , vol.48 , pp. 675-690
    • Kozak, J.J.1    Knight, W.S.2    Kauzmann, W.3
  • 31
    • 0030994063 scopus 로고    scopus 로고
    • Activity and activity coefficient of water in aqueous solutions and their relationships with solution structure parameters
    • O. Miyawaki, A. Saito, T. Matsuo, and K. Nakamura Activity and activity coefficient of water in aqueous solutions and their relationships with solution structure parameters Biosci. Biotechnol. Biochem. 61 1997 466 469 (Pubitemid 27213578)
    • (1997) Bioscience, Biotechnology and Biochemistry , vol.61 , Issue.3 , pp. 466-469
    • Miyawaki, O.1    Saito, A.2    Matsuo, T.3    Nakamura, K.4
  • 32
    • 0034233776 scopus 로고    scopus 로고
    • Theoretic information approach to protein stabilization by solvent engineering
    • R.D. Domenico, R. Lavecchia, and A. Ottavi Theoretic information approach to protein stabilization by solvent engineering AIChE J 46 2000 1478 1489 (Pubitemid 30602688)
    • (2000) AIChE Journal , vol.46 , Issue.7 , pp. 1478-1489
    • Di Domenico, R.1    Lavecchia, R.2    Ottavi, A.3
  • 33
  • 34
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • J.C. Lee, and S.N. Timasheff The stabilization of proteins by sucrose J. Biol. Chem. 256 1981 7193 7201
    • (1981) J. Biol. Chem. , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 35
    • 0023046618 scopus 로고
    • Interaction of calf skin collagen with glycerol: Linked function analysis
    • G.C. Na Interaction of calf skin collagen with glycerol: linked function analysis Biochemistry 25 1986 967 973
    • (1986) Biochemistry , vol.25 , pp. 967-973
    • Na, G.C.1
  • 36
    • 0030973690 scopus 로고    scopus 로고
    • The thermodynamic mechanism of protein stabilization by trehalose
    • DOI 10.1016/S0301-4622(96)02222-3, PII S0301462296022223
    • G. Xie, and S.N. Timasheff The thermodynamic mechanism of protein stabilization by trehalose Biophys. Chem. 64 1997 25 43 (Pubitemid 27148654)
    • (1997) Biophysical Chemistry , vol.64 , Issue.1-3 , pp. 25-43
    • Xie, G.1    Timasheff, S.N.2
  • 37
    • 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
  • 38
    • 23644438008 scopus 로고    scopus 로고
    • D, the Gibbs energy of stabilisation of proteins at different pH values
    • DOI 10.1016/j.bpc.2005.04.004, PII S0301462205000840
    • D, the Gibbs energy of stabilization of proteins at different pH values Biophys. Chem. 117 2005 1 12 (Pubitemid 41116845)
    • (2005) Biophysical Chemistry , vol.117 , Issue.1 , pp. 1-12
    • Haque, I.1    Singh, R.2    Moosavi-Movahedi, A.A.3    Ahmad, F.4
  • 39
    • 55749108344 scopus 로고    scopus 로고
    • D, the Gibbs energy of stabilization of the protein at different pH values: Is the sum effect of monosaccharide individually additive in a mixture?
    • D, the Gibbs energy of stabilization of the protein at different pH values: is the sum effect of monosaccharide individually additive in a mixture? Biophys. Chem. 138 2008 120 129
    • (2008) Biophys. Chem. , vol.138 , pp. 120-129
    • Poddar, N.K.1    Ansari, Z.A.2    Singh, R.K.B.3    Moosavi-Movahedi, A.A.4    Ahmad, F.5
  • 40
    • 33847184181 scopus 로고    scopus 로고
    • Stability of proteins in the presence of carbohydrates; Experiments and modeling using scaled particle theory
    • T.F. O'Connor, P.G. Debenedetti, and J.F. Carbeck Stability of proteins in the presence of carbohydrates; experiments and modeling using scaled particle theory Biophys. Chem. 127 2007 51 63
    • (2007) Biophys. Chem. , vol.127 , pp. 51-63
    • O'Connor, T.F.1    Debenedetti, P.G.2    Carbeck, J.F.3
  • 41
    • 0016292941 scopus 로고
    • Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin
    • R.F. Greene, and N. Pace Urea and guanidine hydrochloride 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
    • Greene, R.F.1    Pace, N.2
  • 42
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • C.N. Pace Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol. 131 1986 266 280 (Pubitemid 16002205)
    • (1986) Methods in Enzymology , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 45
    • 0029896525 scopus 로고    scopus 로고
    • Guanidine hydrochloride unfolding of peptide helices: Separation of denaturant and salt effects
    • DOI 10.1021/bi960341i
    • J.S. Smith, and J.M. Scholtz Guanidine hydrochloride unfolding of peptide helices: separation of denaturant and salt effects Biochemistry 35 1996 7292 7297 (Pubitemid 26182123)
    • (1996) Biochemistry , vol.35 , Issue.22 , pp. 7292-7297
    • Smith, J.S.1    Scholtz, J.M.2
  • 46
    • 0031038733 scopus 로고    scopus 로고
    • Global analysis of the acid-induced and urea-induced unfolding of staphylococcal nuclease and two of its variants
    • DOI 10.1021/bi9609681
    • R.M. Ionescu, and M.R. Eftink Global analysis of the acid-induced and urea-induced unfolding of staphylococcal nuclease and two of its variants Biochemistry 36 1997 1129 1140 (Pubitemid 27076374)
    • (1997) Biochemistry , vol.36 , Issue.5 , pp. 1129-1140
    • Ionescu, R.M.1    Eftink, M.R.2
  • 47
    • 0033592945 scopus 로고    scopus 로고
    • Applicability of urea in the thermodynamic analysis of secondary and tertiary RNA folding
    • V.M. Shelton, T.R. Sosnick, and T. Pan Applicability of urea in the thermodynamic analysis of secondary and tertiary RNA folding Biochemistry 38 1999 16831 16839
    • (1999) Biochemistry , vol.38 , pp. 16831-16839
    • Shelton, V.M.1    Sosnick, T.R.2    Pan, T.3
  • 48
    • 32044437134 scopus 로고    scopus 로고
    • Stability of proteins in the presence of polyols estimated from their guanidinium chloride-induced transition curves at different pH values and 25°C
    • DOI 10.1016/j.bpc.2005.09.016, PII S0301462205002346
    • I. Haque, A. Islam, R. Singh, A.A. Moosavi-Movahedi, and F. Ahmad Stability of proteins in the presence of polyols estimated from their guanidinium chloride-induced transition curves at different pH values and 25 C Biophys. Chem. 119 2006 224 233 (Pubitemid 43202270)
    • (2006) Biophysical Chemistry , vol.119 , Issue.3 , pp. 224-233
    • Haque, I.1    Islam, A.2    Singh, R.3    Moosavi-Movahedi, A.A.4    Ahmad, F.5
  • 49
    • 0032536194 scopus 로고    scopus 로고
    • Group additive contributions to the alcohol-induced α-helix formation of melittin: Implication for the mechanism of the alcohol effects on proteins
    • DOI 10.1006/jmbi.1997.1468
    • N. Hirota, K. Mizuno, and Y. Goto Group additive contributions to the alcohol-induced α-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins J. Mol. Biol. 275 1998 365 378 (Pubitemid 28030010)
    • (1998) Journal of Molecular Biology , vol.275 , Issue.2 , pp. 365-378
    • Hirota, N.1    Mizuno, K.2    Goto, Y.3
  • 50
    • 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 (Pubitemid 36753621)
    • (2003) Biophysical Journal , vol.85 , Issue.1 , pp. 108-125
    • Schellman, J.A.1
  • 51
    • 20544461199 scopus 로고    scopus 로고
    • Thermodynamics of protein interactions with urea and guanidine hydrochloride
    • G.I. Makhatadze Thermodynamics of protein interactions with urea and guanidine hydrochloride J. Phys. Chem. B 103 1999 4781 4785
    • (1999) J. Phys. Chem. B , vol.103 , pp. 4781-4785
    • Makhatadze, G.I.1
  • 52
    • 0037470574 scopus 로고    scopus 로고
    • Effect of dextran on protein stability and conformation attributed to macromolecular crowding
    • DOI 10.1016/S0022-2836(02)01443-2
    • K. Sasahara, P. McPhie, and A.P. Minton Effect of dextran on protein stability and conformation attributed to macromolecule crowding J. Mol. Biol. 326 2003 1227 1237 (Pubitemid 36263394)
    • (2003) Journal of Molecular Biology , vol.326 , Issue.4 , pp. 1227-1237
    • Sasahara, K.1    McPhie, P.2    Minton, A.P.3


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