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Volumn 148, Issue 1-3, 2010, Pages 144-147

Effects of buffer ionization in protein transition volumes

Author keywords

Abnormally titrating groups; Buffer ionization; Proteins; Thermodynamics; Volume

Indexed keywords

BUFFER; GLOBULAR PROTEIN; LYSOZYME; RIBONUCLEASE A;

EID: 77951975694     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2010.03.002     Document Type: Article
Times cited : (13)

References (28)
  • 1
    • 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. 1998, 8:657-664.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 657-664
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 3
    • 62449171817 scopus 로고    scopus 로고
    • Hydration, cavities and volume in protein folding, aggregation and amyloid assembly
    • Silva J.L., Foguel D. Hydration, cavities and volume in protein folding, aggregation and amyloid assembly. Phys. Biol. 2009, 6.
    • (2009) Phys. Biol. , vol.6
    • Silva, J.L.1    Foguel, D.2
  • 4
    • 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 2002, 1595:201-209.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 201-209
    • Royer, C.A.1
  • 5
    • 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. 2001, 26:612-618.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 612-618
    • Silva, J.L.1    Foguel, D.2    Royer, C.A.3
  • 6
    • 33847312741 scopus 로고    scopus 로고
    • Towards an understanding of the temperature/pressure configurational and free-energy landscape of biomolecules
    • Winter R., Lopes D., Grudzielanek S., Vogtt K. Towards an understanding of the temperature/pressure configurational and free-energy landscape of biomolecules. J. Non-Equilibrium Therm. 2007, 32:41-97.
    • (2007) J. Non-Equilibrium Therm. , vol.32 , pp. 41-97
    • Winter, R.1    Lopes, D.2    Grudzielanek, S.3    Vogtt, K.4
  • 7
    • 0017429069 scopus 로고
    • Areas, volumes, packing, and protein-structure
    • Richards F.M. Areas, volumes, packing, and protein-structure. Annu. Rev. Biophys. Bioeng. 1977, 6:151-176.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 8
    • 70449639550 scopus 로고    scopus 로고
    • Origins of pressure-induced protein transitions
    • Chalikian T.V., Macgregor R.B. Origins of pressure-induced protein transitions. J. Mol. Biol. 2009, 394:834-842.
    • (2009) J. Mol. Biol. , vol.394 , pp. 834-842
    • Chalikian, T.V.1    Macgregor, R.B.2
  • 9
    • 33749046141 scopus 로고    scopus 로고
    • Origins of life and biochemistry under high-pressure conditions
    • Daniel I., Oger P., Winter R. Origins of life and biochemistry under high-pressure conditions. Chem. Soc. Rev. 2006, 35:858-875.
    • (2006) Chem. Soc. Rev. , vol.35 , pp. 858-875
    • Daniel, I.1    Oger, P.2    Winter, R.3
  • 10
    • 0036498720 scopus 로고    scopus 로고
    • Determination of the volumetric properties of proteins and other solutes using pressure perturbation calorimetry
    • Lin L.N., Brandts J.F., Brandts J.M., Plotnikov V. Determination of the volumetric properties of proteins and other solutes using pressure perturbation calorimetry. Anal. Biochem. 2002, 302:144-160.
    • (2002) Anal. Biochem. , vol.302 , pp. 144-160
    • Lin, L.N.1    Brandts, J.F.2    Brandts, J.M.3    Plotnikov, V.4
  • 11
    • 0036197878 scopus 로고    scopus 로고
    • Application of pressure perturbation calorimetry to lipid bilayers
    • Heerklotz H., Seelig J. Application of pressure perturbation calorimetry to lipid bilayers. Biophys. J. 2002, 82:1445-1452.
    • (2002) Biophys. J. , vol.82 , pp. 1445-1452
    • Heerklotz, H.1    Seelig, J.2
  • 13
    • 72749109890 scopus 로고    scopus 로고
    • Use of pressure perturbation calorimetry to characterize the volumetric properties of proteins
    • Schweiker K.L., Makhatadze G.I. Use of pressure perturbation calorimetry to characterize the volumetric properties of proteins. Methods Enzymol. 2009, 527-547.
    • (2009) Methods Enzymol. , pp. 527-547
    • Schweiker, K.L.1    Makhatadze, G.I.2
  • 14
    • 72749118055 scopus 로고    scopus 로고
    • Universal convergence of the specific volume changes of globular proteins upon unfolding
    • Schweiker K.L., Fitz V.W., Makhatadze G.I. Universal convergence of the specific volume changes of globular proteins upon unfolding. Biochemistry 2009, 48:10846-10851.
    • (2009) Biochemistry , vol.48 , pp. 10846-10851
    • Schweiker, K.L.1    Fitz, V.W.2    Makhatadze, G.I.3
  • 15
    • 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 1996, 39:619-626.
    • (1996) Biopolymers , vol.39 , pp. 619-626
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 16
    • 0038487378 scopus 로고    scopus 로고
    • How large are the volume changes accompanying protein transitions and binding?
    • Chalikian T.V., Filfil R. How large are the volume changes accompanying protein transitions and binding?. Biophys. Chem. 2003, 104:489-499.
    • (2003) Biophys. Chem. , vol.104 , pp. 489-499
    • Chalikian, T.V.1    Filfil, R.2
  • 17
    • 0000818472 scopus 로고
    • Reaction volume of protonic ionization for buffering agents. Prediction of pressure-dependence of pH and pOH.
    • Kitamura Y., Itoh T. Reaction volume of protonic ionization for buffering agents. Prediction of pressure-dependence of pH and pOH. J. Solution Chem. 1987, 16:715-725.
    • (1987) J. Solution Chem. , vol.16 , pp. 715-725
    • Kitamura, Y.1    Itoh, T.2
  • 18
    • 0015153612 scopus 로고
    • Statistical thermodynamics of nucleic acid melting transitions with coupled binding equilibria
    • Crothers D.M. Statistical thermodynamics of nucleic acid melting transitions with coupled binding equilibria. Biopolymers 1971, 10:2147-2160.
    • (1971) Biopolymers , vol.10 , pp. 2147-2160
    • Crothers, D.M.1
  • 19
    • 41449085127 scopus 로고    scopus 로고
    • Partial molar volumes and adiabatic compressibilities of unfolded protein states
    • Lee S., Tikhomirova A., Shalvardjian N., Chalikian T.V. Partial molar volumes and adiabatic compressibilities of unfolded protein states. Biophys. Chem. 2008, 134:185-199.
    • (2008) Biophys. Chem. , vol.134 , pp. 185-199
    • Lee, S.1    Tikhomirova, A.2    Shalvardjian, N.3    Chalikian, T.V.4
  • 20
    • 0016682964 scopus 로고
    • PH-dependence of thermodynamics of interaction of 3'-cytidine monophosphate with ribonuclease A
    • Flogel M., Biltonen R.L. pH-dependence of thermodynamics of interaction of 3'-cytidine monophosphate with ribonuclease A. Biochemistry 1975, 14:2610-2615.
    • (1975) Biochemistry , vol.14 , pp. 2610-2615
    • Flogel, M.1    Biltonen, R.L.2
  • 21
    • 0026808783 scopus 로고
    • Peptide binding to lipid bilayers. Nonclassical hydrophobic effect and membrane-induced pKa shifts.
    • Beschiaschvili G., Seelig J. Peptide binding to lipid bilayers. Nonclassical hydrophobic effect and membrane-induced pKa shifts. Biochemistry 1992, 31:10044-10053.
    • (1992) Biochemistry , vol.31 , pp. 10044-10053
    • Beschiaschvili, G.1    Seelig, J.2
  • 22
    • 0031547981 scopus 로고    scopus 로고
    • Dissecting the energetics of a protein-protein interaction: the binding of ovomucoid third domain to elastase
    • Baker B.M., Murphy K.P. Dissecting the energetics of a protein-protein interaction: the binding of ovomucoid third domain to elastase. J. Mol. Biol. 1997, 268:557-569.
    • (1997) J. Mol. Biol. , vol.268 , pp. 557-569
    • Baker, B.M.1    Murphy, K.P.2
  • 23
    • 0018588511 scopus 로고
    • Stability of proteins: small globular proteins
    • Privalov P.L. Stability of proteins: small globular proteins. Adv. Protein Chem. 1979, 33:167-241.
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 24
    • 0343247668 scopus 로고    scopus 로고
    • The native and the heat-induced denatured states of α-chymotrypsinogen A: thermodynamic and spectroscopic studies
    • Chalikian T.V., Volker J., Anafi D., Breslauer K.J. The native and the heat-induced denatured states of α-chymotrypsinogen A: thermodynamic and spectroscopic studies. J. Mol. Biol. 1997, 274:237-252.
    • (1997) J. Mol. Biol. , vol.274 , pp. 237-252
    • Chalikian, T.V.1    Volker, J.2    Anafi, D.3    Breslauer, K.J.4
  • 25
    • 0014937559 scopus 로고
    • Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme
    • Saxena V.P., Wetlaufer D.B. Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry 1970, 9:5015-5023.
    • (1970) Biochemistry , vol.9 , pp. 5015-5023
    • Saxena, V.P.1    Wetlaufer, D.B.2
  • 26
    • 0014288823 scopus 로고
    • Binding of phosphate ligands to ribonuclease A
    • Anderson D.G., Hammes G.G., Walz F.G. Binding of phosphate ligands to ribonuclease A. Biochemistry 1968, 7:1637-1645.
    • (1968) Biochemistry , vol.7 , pp. 1637-1645
    • Anderson, D.G.1    Hammes, G.G.2    Walz, F.G.3
  • 27
    • 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., Breslauer K.J. The hydration of globular proteins as derived from volume and compressibility measurements: cross correlating thermodynamic and structural data. J. Mol. Biol. 1996, 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
  • 28
    • 0023406843 scopus 로고
    • Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves
    • Marky L.A., Breslauer K.J. Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves. Biopolymers 1987, 26:1601-1620.
    • (1987) Biopolymers , vol.26 , pp. 1601-1620
    • Marky, L.A.1    Breslauer, K.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.