메뉴 건너뛰기




Volumn 52, Issue 4, 2013, Pages 672-680

Interactions of glycine betaine with proteins: Insights from volume and compressibility measurements

Author keywords

[No Author keywords available]

Indexed keywords

ADIABATIC COMPRESSIBILITY; ASSOCIATION CONSTANT; BINDING REACTIONS; CAVITY FORMATION; CHANGES IN VOLUME; COMPRESSIBILITY MEASUREMENTS; CONFORMATIONAL TRANSITIONS; COOPERATIVE EFFECTS; COSOLVENTS; CYTOCHROME C; ENERGETIC PROPERTIES; EXCLUDED VOLUME EFFECTS; GLOBULAR PROTEINS; GLYCINE BETAINE; IDEAL SOLUTIONS; LOW-MOLECULAR WEIGHT; NATIVE STATE; OSMOLYTES; OVALBUMINS; PARTIAL MOLAR VOLUME; RIBONUCLEASE A; STATISTICAL THERMODYNAMIC MODELS; VOLUMETRIC DATA; WATER MOLECULE;

EID: 84873818542     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301554h     Document Type: Article
Times cited : (23)

References (47)
  • 1
    • 0026788012 scopus 로고
    • Water as ligand: PPreferential binding and exclusion of denaturants in protein unfolding
    • Timasheff, S. N. (1992) Water as ligand: pPreferential binding and exclusion of denaturants in protein unfolding Biochemistry 31, 9857-9864
    • (1992) Biochemistry , vol.31 , pp. 9857-9864
    • Timasheff, S.N.1
  • 2
    • 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
  • 3
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff, S. N. (1998) Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated Adv. Protein Chem. 51, 355-432
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 4
    • 0037137253 scopus 로고    scopus 로고
    • Protein hydration, thermodynamic binding, and preferential hydration
    • Timasheff, S. N. (2002) Protein hydration, thermodynamic binding, and preferential hydration Biochemistry 41, 13473-13482
    • (2002) Biochemistry , vol.41 , pp. 13473-13482
    • Timasheff, S.N.1
  • 5
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • Yancey, P. H., Clark, M. E., Hand, S. C., Bowlus, R. D., and Somero, G. N. (1982) Living with water stress: Evolution of osmolyte systems Science 217, 1214-1222
    • (1982) Science , vol.217 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 6
    • 24644450812 scopus 로고    scopus 로고
    • Organic osmolytes as compatible, metabolic and counteracting cytoprotectants in high osmolarity and other stresses
    • Yancey, P. H. (2005) Organic osmolytes as compatible, metabolic and counteracting cytoprotectants in high osmolarity and other stresses J. Exp. Biol. 208, 2819-2830
    • (2005) J. Exp. Biol. , vol.208 , pp. 2819-2830
    • Yancey, P.H.1
  • 7
    • 0344653612 scopus 로고    scopus 로고
    • Responses of E. coli to osmotic stress: Large changes in amounts of cytoplasmic solutes and water
    • Record, M. T., Jr., Courtenay, E. S., Cayley, D. S., and Guttman, H. J. (1998) Responses of E. coli to osmotic stress: Large changes in amounts of cytoplasmic solutes and water Trends Biochem. Sci. 23, 143-148
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 143-148
    • Record, M.T.1    Courtenay, E.S.2    Cayley, D.S.3    Guttman, H.J.4
  • 8
    • 0032079008 scopus 로고    scopus 로고
    • Biophysical compensation mechanisms buffering E. coli protein-nucleic acid interactions against changing environments
    • Record, M. T., Jr., Courtenay, E. S., Cayley, S., and Guttman, H. J. (1998) Biophysical compensation mechanisms buffering E. coli protein-nucleic acid interactions against changing environments Trends Biochem. Sci. 23, 190-194
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 190-194
    • Record Jr., M.T.1    Courtenay, E.S.2    Cayley, S.3    Guttman, H.J.4
  • 9
    • 0038311869 scopus 로고    scopus 로고
    • Protein stability in mixed solvents: A balance of contact interaction and excluded volume
    • Schellman, J. A. (2003) Protein stability in mixed solvents: A balance of contact interaction and excluded volume Biophys. J. 85, 108-125
    • (2003) Biophys. J. , vol.85 , pp. 108-125
    • Schellman, J.A.1
  • 10
    • 3142655877 scopus 로고    scopus 로고
    • Application of the local-bulk partitioning and competitive binding models to interpret preferential interactions of glycine betaine and urea with protein surface
    • Felitsky, D. J. and Record, M. T. (2004) Application of the local-bulk partitioning and competitive binding models to interpret preferential interactions of glycine betaine and urea with protein surface Biochemistry 43, 9276-9288
    • (2004) Biochemistry , vol.43 , pp. 9276-9288
    • Felitsky, D.J.1    Record, M.T.2
  • 11
    • 70350513011 scopus 로고    scopus 로고
    • Interactions of the osmolyte glycine betaine with molecular surfaces in water: Thermodynamics, structural interpretation, and prediction of m-values
    • Capp, M. W., Pegram, L. M., Saecker, R. M., Kratz, M., Riccardi, D., Wendorff, T., Cannon, J. G., and Record, M. T. (2009) Interactions of the osmolyte glycine betaine with molecular surfaces in water: Thermodynamics, structural interpretation, and prediction of m-values Biochemistry 48, 10372-10379
    • (2009) Biochemistry , vol.48 , pp. 10372-10379
    • Capp, M.W.1    Pegram, L.M.2    Saecker, R.M.3    Kratz, M.4    Riccardi, D.5    Wendorff, T.6    Cannon, J.G.7    Record, M.T.8
  • 12
    • 57049105810 scopus 로고    scopus 로고
    • Structural thermodynamics of protein preferential solvation: Osmolyte solvation of proteins, aminoacids, and peptides
    • Auton, M., Bolen, D. W., and Rosgen, J. (2008) Structural thermodynamics of protein preferential solvation: Osmolyte solvation of proteins, aminoacids, and peptides Proteins: Struct., Funct., Bioinf. 73, 802-813
    • (2008) Proteins: Struct., Funct., Bioinf. , vol.73 , pp. 802-813
    • Auton, M.1    Bolen, D.W.2    Rosgen, J.3
  • 13
    • 46449109015 scopus 로고    scopus 로고
    • Structure and energetics of the hydrogen-bonded backbone in protein folding
    • Bolen, D. W. and Rose, G. D. (2008) Structure and energetics of the hydrogen-bonded backbone in protein folding Annu. Rev. Biochem. 77, 339-362
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 339-362
    • Bolen, D.W.1    Rose, G.D.2
  • 14
    • 35748981504 scopus 로고    scopus 로고
    • Application of the transfer model to understand how naturally occuring osmolytes affect protein stability
    • Auton, M. and Bolen, D. W. (2007) Application of the transfer model to understand how naturally occuring osmolytes affect protein stability Methods Enzymol. 428, 397-418
    • (2007) Methods Enzymol. , vol.428 , pp. 397-418
    • Auton, M.1    Bolen, D.W.2
  • 15
    • 0036099038 scopus 로고    scopus 로고
    • Assessing accumulated solvent near a macromolecular solute by preferential interaction coefficients
    • Tang, K. E. and Bloomfield, V. A. (2002) Assessing accumulated solvent near a macromolecular solute by preferential interaction coefficients Biophys. J. 82, 2876-2891
    • (2002) Biophys. J. , vol.82 , pp. 2876-2891
    • Tang, K.E.1    Bloomfield, V.A.2
  • 17
    • 65249118310 scopus 로고    scopus 로고
    • Volumetric properties of solvation in binary solvents
    • Lee, S. Y. and Chalikian, T. V. (2009) Volumetric properties of solvation in binary solvents J. Phys. Chem. B 113, 2443-2450
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2443-2450
    • Lee, S.Y.1    Chalikian, T.V.2
  • 18
    • 77956142105 scopus 로고    scopus 로고
    • Urea interactions with protein groups: A volumetric study
    • Lee, S., Shek, Y. L., and Chalikian, T. V. (2010) Urea interactions with protein groups: A volumetric study Biopolymers 93, 866-879
    • (2010) Biopolymers , vol.93 , pp. 866-879
    • Lee, S.1    Shek, Y.L.2    Chalikian, T.V.3
  • 19
    • 79955962032 scopus 로고    scopus 로고
    • Volumetric measurements in binary solvents: Theory to experiment
    • Chalikian, T. V. (2011) Volumetric measurements in binary solvents: Theory to experiment Biophys. Chem. 156, 3-12
    • (2011) Biophys. Chem. , vol.156 , pp. 3-12
    • Chalikian, T.V.1
  • 20
    • 80053413194 scopus 로고    scopus 로고
    • Volumetric characterization of interactions of glycine betaine with protein groups
    • Shek, Y. L. and Chalikian, T. V. (2011) Volumetric characterization of interactions of glycine betaine with protein groups J. Phys. Chem. B 115, 11481-11489
    • (2011) J. Phys. Chem. B , vol.115 , pp. 11481-11489
    • Shek, Y.L.1    Chalikian, T.V.2
  • 21
    • 0342487512 scopus 로고
    • Solubility of amino acids in aqueous urea solutions and its implications for the denaturation of proteins by urea
    • Whitney, P. L. and Tanford, C. (1962) Solubility of amino acids in aqueous urea solutions and its implications for the denaturation of proteins by urea J. Biol. Chem. 237, 1735-1737
    • (1962) J. Biol. Chem. , vol.237 , pp. 1735-1737
    • Whitney, P.L.1    Tanford, C.2
  • 22
    • 78651119214 scopus 로고
    • The solubility of amino acids and related compounds in aqueous urea solution
    • Nozaki, Y. and Tanford, C. (1963) The solubility of amino acids and related compounds in aqueous urea solution J. Biol. Chem. 238, 4074-4081
    • (1963) J. Biol. Chem. , vol.238 , pp. 4074-4081
    • Nozaki, Y.1    Tanford, C.2
  • 23
    • 80054717093 scopus 로고    scopus 로고
    • Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer
    • Guinn, E. J., Pegram, L. M., Capp, M. W., Pollock, M. N., and Record, M. T., Jr. (2011) Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer Proc. Natl. Acad. Sci. U.S.A. 108, 16932-16937
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 16932-16937
    • Guinn, E.J.1    Pegram, L.M.2    Capp, M.W.3    Pollock, M.N.4    Record Jr., M.T.5
  • 24
    • 0015700007 scopus 로고
    • Ultrasonic measurements with milliliter liquid samples in 0.5-100 MHz range
    • Eggers, F. and Funck, T. (1973) Ultrasonic measurements with milliliter liquid samples in 0.5-100 MHz range Rev. Sci. Instrum. 44, 969-977
    • (1973) Rev. Sci. Instrum. , vol.44 , pp. 969-977
    • Eggers, F.1    Funck, T.2
  • 25
    • 0020156572 scopus 로고
    • Development of methods of precise ultrasonic measurements in small volumes of liquids
    • Sarvazyan, A. P. (1982) Development of methods of precise ultrasonic measurements in small volumes of liquids Ultrasonics 20, 151-154
    • (1982) Ultrasonics , vol.20 , pp. 151-154
    • Sarvazyan, A.P.1
  • 26
    • 0000975004 scopus 로고
    • Ultrasonic velocity and attenuation measurements in liquids with resonators, extending the MHz frequency range
    • Eggers, F. (1992) Ultrasonic velocity and attenuation measurements in liquids with resonators, extending the MHz frequency range Acustica 76, 231-240
    • (1992) Acustica , vol.76 , pp. 231-240
    • Eggers, F.1
  • 27
    • 0038914607 scopus 로고    scopus 로고
    • Broad-band ultrasonic measurement techniques for liquids
    • Eggers, F. and Kaatze, U. (1996) Broad-band ultrasonic measurement techniques for liquids Meas. Sci. Technol. 7, 1-19
    • (1996) Meas. Sci. Technol. , vol.7 , pp. 1-19
    • Eggers, F.1    Kaatze, U.2
  • 28
    • 0000977015 scopus 로고
    • Constant-path acoustic interferometer with transition layers for precision measurements in small liquid volumes
    • Sarvazyan, A. P., Selkov, E. E., and Chalikyan, T. V. (1988) Constant-path acoustic interferometer with transition layers for precision measurements in small liquid volumes Acoust. Phys. 34, 631-634
    • (1988) Acoust. Phys. , vol.34 , pp. 631-634
    • Sarvazyan, A.P.1    Selkov, E.E.2    Chalikyan, T.V.3
  • 29
    • 0026131365 scopus 로고
    • Theoretical analysis of an ultrasonic interferometer for precise measurements at high pressures
    • Sarvazyan, A. P. and Chalikian, T. V. (1991) Theoretical analysis of an ultrasonic interferometer for precise measurements at high pressures Ultrasonics 29, 119-124
    • (1991) Ultrasonics , vol.29 , pp. 119-124
    • Sarvazyan, A.P.1    Chalikian, T.V.2
  • 30
    • 0001384941 scopus 로고
    • The velocity of sound in electrolytic solutions
    • Barnartt, S. (1952) The velocity of sound in electrolytic solutions J. Chem. Phys. 20, 278-279
    • (1952) J. Chem. Phys. , vol.20 , pp. 278-279
    • Barnartt, S.1
  • 31
    • 0001054914 scopus 로고
    • Standard partial molal compressibilities by ultrasonics. 1. Sodium chloride and potassium chloride at 25 C
    • Owen, B. B. and Simons, H. L. (1957) Standard partial molal compressibilities by ultrasonics. 1. Sodium chloride and potassium chloride at 25 C J. Phys. Chem. 61, 479-482
    • (1957) J. Phys. Chem. , vol.61 , pp. 479-482
    • Owen, B.B.1    Simons, H.L.2
  • 32
    • 33845561444 scopus 로고
    • Compressibility of globular proteins in water at 25 C
    • Gekko, K. and Noguchi, H. (1979) Compressibility of globular proteins in water at 25 C J. Phys. Chem. 83, 2706-2714
    • (1979) J. Phys. Chem. , vol.83 , pp. 2706-2714
    • Gekko, K.1    Noguchi, H.2
  • 33
    • 0022999267 scopus 로고
    • Compressibility-structure relationship of globular proteins
    • Gekko, K. and Hasegawa, Y. (1986) Compressibility-structure relationship of globular proteins Biochemistry 25, 6563-6571
    • (1986) Biochemistry , vol.25 , pp. 6563-6571
    • Gekko, K.1    Hasegawa, Y.2
  • 34
    • 0008047756 scopus 로고    scopus 로고
    • The hydration of globular proteins as derived from volume and compressibility measurements: Cross correlating thermodynamic and structural data
    • Chalikian, T. V., Totrov, M., Abagyan, R., and Breslauer, K. J. (1996) The hydration of globular proteins as derived from volume and compressibility measurements: Cross correlating thermodynamic and structural data J. Mol. Biol. 260, 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
  • 35
    • 33747754400 scopus 로고
    • Scaled particle theory of aqueous and non-aqueous solutions
    • Pierotti, R. A. (1976) Scaled particle theory of aqueous and non-aqueous solutions Chem. Rev. 76, 717-726
    • (1976) Chem. Rev. , vol.76 , pp. 717-726
    • Pierotti, R.A.1
  • 36
    • 0001376481 scopus 로고
    • Enthalpies, heat capacities, and volumes of transfer of tetrabutylammonium ion from water to aqueous mixed solvents from point of view of scaled particle theory
    • Desrosiers, N. and Desnoyers, J. E. (1976) Enthalpies, heat capacities, and volumes of transfer of tetrabutylammonium ion from water to aqueous mixed solvents from point of view of scaled particle theory Can. J. Chem. 54, 3800-3808
    • (1976) Can. J. Chem. , vol.54 , pp. 3800-3808
    • Desrosiers, N.1    Desnoyers, J.E.2
  • 37
    • 0033746785 scopus 로고    scopus 로고
    • Excluded volume in solvation: Sensitivity of scaled-particle theory to solvent size and density
    • Tang, K. E. S. and Bloomfield, V. A. (2000) Excluded volume in solvation: Sensitivity of scaled-particle theory to solvent size and density Biophys. J. 79, 2222-2234
    • (2000) Biophys. J. , vol.79 , pp. 2222-2234
    • Tang, K.E.S.1    Bloomfield, V.A.2
  • 38
    • 33750943209 scopus 로고    scopus 로고
    • Cavity contact correlation function of water from scaled particle theory
    • Graziano, G. (2006) Cavity contact correlation function of water from scaled particle theory Chem. Phys. Lett. 432, 84-87
    • (2006) Chem. Phys. Lett. , vol.432 , pp. 84-87
    • Graziano, G.1
  • 39
    • 57249109776 scopus 로고    scopus 로고
    • Apparent molar isentropic compressions and expansions of solutions
    • Blandamer, M. J., Davis, M. I., Douheret, G., and Reis, J. C. R. (2001) Apparent molar isentropic compressions and expansions of solutions Chem. Soc. Rev. 30, 8-15
    • (2001) Chem. Soc. Rev. , vol.30 , pp. 8-15
    • Blandamer, M.J.1    Davis, M.I.2    Douheret, G.3    Reis, J.C.R.4
  • 40
    • 0027993455 scopus 로고
    • Hydration and partial compressibility of biological compounds
    • Chalikian, T. V., Sarvazyan, A. P., and Breslauer, K. J. (1994) Hydration and partial compressibility of biological compounds Biophys. Chem. 51, 89-107
    • (1994) Biophys. Chem. , vol.51 , pp. 89-107
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Breslauer, K.J.3
  • 41
    • 0031790423 scopus 로고    scopus 로고
    • Thermodynamic analysis of biomolecules: A volumetric approach
    • Chalikian, T. V. and Breslauer, K. J. (1998) Thermodynamic analysis of biomolecules: A volumetric approach Curr. Opin. Struct. Biol. 8, 657-664
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 657-664
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 42
  • 44
    • 27244437952 scopus 로고    scopus 로고
    • Predicting the energetics of osmolyte-induced protein folding/unfolding
    • Auton, M. and Bolen, D. W. (2005) Predicting the energetics of osmolyte-induced protein folding/unfolding Proc. Natl. Acad. Sci. U.S.A. 102, 15065-15068
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15065-15068
    • Auton, M.1    Bolen, D.W.2
  • 45
    • 34848916114 scopus 로고    scopus 로고
    • Anatomy of energetic changes accompanying urea-induced protein denaturation
    • Auton, M., Holthauzen, L. M., and Bolen, D. W. (2007) Anatomy of energetic changes accompanying urea-induced protein denaturation Proc. Natl. Acad. Sci. U.S.A. 104, 15317-15322
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 15317-15322
    • Auton, M.1    Holthauzen, L.M.2    Bolen, D.W.3
  • 46
    • 80052319202 scopus 로고    scopus 로고
    • Osmolyte effects on protein stability and solubility: A balancing act between backbone and side-chains
    • Auton, M., Rosgen, J., Sinev, M., Holthauzen, L. M., and Bolen, D. W. (2011) Osmolyte effects on protein stability and solubility: A balancing act between backbone and side-chains Biophys. Chem. 159, 90-99
    • (2011) Biophys. Chem. , vol.159 , pp. 90-99
    • Auton, M.1    Rosgen, J.2    Sinev, M.3    Holthauzen, L.M.4    Bolen, D.W.5
  • 47
    • 0020790862 scopus 로고
    • Preferential interactions of proteins with solvent components in aqueous amino acid solutions
    • Arakawa, T. and Timasheff, S. N. (1983) Preferential interactions of proteins with solvent components in aqueous amino acid solutions Arch. Biochem. Biophys. 224, 169-177
    • (1983) Arch. Biochem. Biophys. , vol.224 , pp. 169-177
    • Arakawa, T.1    Timasheff, S.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.