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Volumn 71, Issue 4, 1996, Pages 2049-2055

Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CALORIMETRY; CRYSTALLIZATION; ENTHALPY; LIGAND BINDING; MATHEMATICAL COMPUTING; PH; PROTEIN BINDING; PROTON TRANSPORT; THEORY; TITRIMETRY;

EID: 0029832524     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79403-1     Document Type: Article
Times cited : (282)

References (25)
  • 1
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • Baldwin , R. L. 1986. Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl. Acad. Sci. USA. 83:8069-8072.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8069-8072
    • Baldwin, R.L.1
  • 5
    • 0026651279 scopus 로고
    • Heat capacity changes and hydrophobic interactions in the binding of FK506 and rapamycin to the FK506 binding protein
    • Connelly, P. R., and J. A. Thomson. 1992. Heat capacity changes and hydrophobic interactions in the binding of FK506 and rapamycin to the FK506 binding protein. Proc. Natl. Acad. Sci. USA. 89:4781-4785.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4781-4785
    • Connelly, P.R.1    Thomson, J.A.2
  • 6
    • 0025293251 scopus 로고
    • Thermodynamics of protein-peptide interactions in the ribonuclease S system studied by titration calorimetry
    • Connelly, P. R., R. Varadarajan, J. M. Sturtevant, and F. M. Richards. 1990. Thermodynamics of protein-peptide interactions in the ribonuclease S system studied by titration calorimetry. Biochemistry. 29:6108-6114.
    • (1990) Biochemistry , vol.29 , pp. 6108-6114
    • Connelly, P.R.1    Varadarajan, R.2    Sturtevant, J.M.3    Richards, F.M.4
  • 7
    • 0025706147 scopus 로고
    • The meaning of hydrophobicity
    • Dill, K. A. 1990. The meaning of hydrophobicity. Science. 250:297.
    • (1990) Science , vol.250 , pp. 297
    • Dill, K.A.1
  • 8
    • 0029131539 scopus 로고
    • Tight binding affinities determined from thetmodynamic linkage to protons by titration calorimetry
    • Doyle, M. L., G. Louie, P. Del Monte, and T. Sokoloski. 1995. Tight binding affinities determined from thetmodynamic linkage to protons by titration calorimetry. Methods Enzymol. 259:183-194.
    • (1995) Methods Enzymol , vol.259 , pp. 183-194
    • Doyle, M.L.1    Louie, G.2    Del Monte, P.3    Sokoloski, T.4
  • 9
    • 0021093448 scopus 로고
    • Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: General thermodynamic models and data for the binding of nucleotides to ribonuclease A
    • Eftink, M. R., A. C. Anusiem, and R. L. Biltonen. 1983. Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: general thermodynamic models and data for the binding of nucleotides to ribonuclease A. Biochemistry. 22:3884-3896.
    • (1983) Biochemistry , vol.22 , pp. 3884-3896
    • Eftink, M.R.1    Anusiem, A.C.2    Biltonen, R.L.3
  • 10
    • 0000873192 scopus 로고
    • Thermodynamics of interacting biological systems
    • A. E. Beezer, editor. Academic Press, San Diego
    • Eftink, M., and R. Biltonen. 1980. Thermodynamics of interacting biological systems. In Biological Microcalorimetry. A. E. Beezer, editor. Academic Press, San Diego. 343-412.
    • (1980) Biological Microcalorimetry , pp. 343-412
    • Eftink, M.1    Biltonen, R.2
  • 12
    • 0000013706 scopus 로고
    • An equation of state describing hydrophobic interactions
    • Gill, S. J., and I. Wadsö. 1976. An equation of state describing hydrophobic interactions. Proc. Natl. Acad. Sci. USA. 73:2955-2958.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2955-2958
    • Gill, S.J.1    Wadsö, I.2
  • 13
    • 0029080864 scopus 로고
    • Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin
    • Gómez, J., and E. Freire. 1995. Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin. J. Mol. Biol. 252:337-350.
    • (1995) J. Mol. Biol. , vol.252 , pp. 337-350
    • Gómez, J.1    Freire, E.2
  • 14
    • 0029042647 scopus 로고
    • Calorimetric studies on the interaction of horse ferricytochrome c and yeast cytochrome c peroxidase
    • Kresheck, G. C., L. B. Vitello, and J. E. Erman. 1995. Calorimetric studies on the interaction of horse ferricytochrome c and yeast cytochrome c peroxidase. Biochemistry. 34:8398-8405.
    • (1995) Biochemistry , vol.34 , pp. 8398-8405
    • Kresheck, G.C.1    Vitello, L.B.2    Erman, J.E.3
  • 15
    • 0025360593 scopus 로고
    • Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: Hydration effect
    • Makhatadze, G. I., and P. L. Privalov. 1990. Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect. J. Mol. Biol. 213:375-384.
    • (1990) J. Mol. Biol. , vol.213 , pp. 375-384
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 16
    • 0028809265 scopus 로고
    • Configurational effects in antibody-antigen interactions determined by micro-calorimetry
    • Murphy, K. P., E. Freire, and Y. Paterson. 1995. Configurational effects in antibody-antigen interactions determined by micro-calorimetry. Proteins. 21:83-90.
    • (1995) Proteins , vol.21 , pp. 83-90
    • Murphy, K.P.1    Freire, E.2    Paterson, Y.3
  • 17
    • 0025098571 scopus 로고
    • Common features of protein unfolding and dissolution of hydrophobic compounds
    • Murphy, K. P., P. L. Privalov, and S. J. Gill. 1990. Common features of protein unfolding and dissolution of hydrophobic compounds. Science. 247:559-561.
    • (1990) Science , vol.247 , pp. 559-561
    • Murphy, K.P.1    Privalov, P.L.2    Gill, S.J.3
  • 18
    • 0027537127 scopus 로고
    • Structural energetics of peptide recognition: Angiotensin II/antibody binding
    • Murphy, K. P., D. Xie, K. C. Garcia, L. M. Amzel, and E. Freire. 1993. Structural energetics of peptide recognition: angiotensin II/antibody binding. Proteins. 15:113-120.
    • (1993) Proteins , vol.15 , pp. 113-120
    • Murphy, K.P.1    Xie, D.2    Garcia, K.C.3    Amzel, L.M.4    Freire, E.5
  • 19
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R. S., and M. T. Record, Jr. 1994. Coupling of local folding to site-specific binding of proteins to DNA. Science. 263:777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 20
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant, J. M. 1977. Heat capacity and entropy changes in processes involving proteins. Proc. Natl. Acad. Sci. USA. 74:2236-2240.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 21
    • 0021961860 scopus 로고
    • Calorimetric studies of the binding of Streptomyces subtilisin inhibitor to subtilisin of Bacillus subtilis strain N'
    • Takahashi, K., and H. Fukada. 1985. Calorimetric studies of the binding of Streptomyces subtilisin inhibitor to subtilisin of Bacillus subtilis strain N'. Biochemistry. 24:297-300.
    • (1985) Biochemistry , vol.24 , pp. 297-300
    • Takahashi, K.1    Fukada, H.2
  • 22
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., S. Williston, J. F. Brandts, and L.-N. Lin. 1989. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179:131-137.
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.-N.4
  • 24
    • 0028289925 scopus 로고
    • Solvent rearrangement in an antigen-antibody interface introduced by sitedirected mutagenesis of the antibody combining site
    • Ysern, X., B. A. Fields, T. N. Bhat, F. A. Goldbaum, W. Dall'Acqua, F. P. Schwarz, R. J. Poljak, and R. A. Mariuzza. 1994. Solvent rearrangement in an antigen-antibody interface introduced by sitedirected mutagenesis of the antibody combining site. J. Mol. Biol. 238:496-500.
    • (1994) J. Mol. Biol. , vol.238 , pp. 496-500
    • Ysern, X.1    Fields, B.A.2    Bhat, T.N.3    Goldbaum, F.A.4    Dall'Acqua, W.5    Schwarz, F.P.6    Poljak, R.J.7    Mariuzza, R.A.8
  • 25
    • 0019333096 scopus 로고
    • A calorimetric comparison of trypsin and its anhydro modification in complex formation with Kunitz soybean inhibitor
    • Yung, B. Y. K., and C. G. Trowbridge. 1980. A calorimetric comparison of trypsin and its anhydro modification in complex formation with Kunitz soybean inhibitor. J. Biol. Chem. 255:9724-9730.
    • (1980) J. Biol. Chem. , vol.255 , pp. 9724-9730
    • Yung, B.Y.K.1    Trowbridge, C.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.