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Volumn 123, Issue 5, 1998, Pages 827-831

Temperature dependency of thermodynamic parameters in interactions between hen egg-white lysozyme (HEL) and anti-HEL antibodies

Author keywords

Differential titration calorimetry; Entropy enthalpy compensation; Heat capacity change; Hydrophobic interactions

Indexed keywords

ANTIBODY; LYSOZYME;

EID: 0031981530     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022011     Document Type: Article
Times cited : (3)

References (16)
  • 2
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • Ross, P.D. and Subramanian, S. (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20, 3096-3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 3
    • 0024378717 scopus 로고
    • Role of the hydrophobic effect in stability of site-specific protein-DNA complexes
    • Ha, J.-H., Spolar, R.S., and Record, Jr., M.T. (1989) Role of the hydrophobic effect in stability of site-specific protein-DNA complexes. J. Mol. Biol. 209, 801-816
    • (1989) J. Mol. Biol. , vol.209 , pp. 801-816
    • Ha, J.-H.1    Spolar, R.S.2    Record Jr., M.T.3
  • 4
    • 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
  • 5
    • 0000180763 scopus 로고
    • Temperature depencence of the hydrophobic interaction in protein folding
    • Baldwin, R.L. (1986) Temperature depencence 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
  • 6
    • 0022519337 scopus 로고
    • Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution
    • Amit, A.G., Mariuzza, R.A, Phillips, S.E.V., and Poljak, R.J. (1986) Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution. Science 233, 747-753
    • (1986) Science , vol.233 , pp. 747-753
    • Amit, A.G.1    Mariuzza, R.A.2    Phillips, S.E.V.3    Poljak, R.J.4
  • 7
    • 0027328372 scopus 로고
    • Effects of substitution of closely related amino acids at the contact surface in an antigen-antibody complex on thermodynamic parameters
    • Ito, W., Iba, Y., and Kurosawa, Y. (1993) Effects of substitution of closely related amino acids at the contact surface in an antigen-antibody complex on thermodynamic parameters. J. Biol. Chem. 268, 16639-16647
    • (1993) J. Biol. Chem. , vol.268 , pp. 16639-16647
    • Ito, W.1    Iba, Y.2    Kurosawa, Y.3
  • 8
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., Williston, S., Brandts, J.F., and Lin, L.-N. (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
  • 10
    • 0026726191 scopus 로고
    • On the origin of the enthalpy and entropy convergence temperatures in protein folding
    • Fu, L. and Freire, E. (1992) On the origin of the enthalpy and entropy convergence temperatures in protein folding. Proc. Natl. Acad. Sci. USA 89, 9335-9338
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9335-9338
    • Fu, L.1    Freire, E.2
  • 11
    • 0026688412 scopus 로고
    • Thermodynamics of oligosaccharide binding to a monoclonal antibody specific for a Salmonella O-antigen point to hydrophobic interactions in the binding site
    • Sigurskjold, B.W. and Bundle, D.R. (1992) Thermodynamics of oligosaccharide binding to a monoclonal antibody specific for a Salmonella O-antigen point to hydrophobic interactions in the binding site. J. Biol. Chem. 267, 8371-8376
    • (1992) J. Biol. Chem. , vol.267 , pp. 8371-8376
    • Sigurskjold, B.W.1    Bundle, D.R.2
  • 12
    • 0023047641 scopus 로고
    • Thermodynamic properties of ligand binding by monoclonal anti-fluorescyl antibodies
    • Herron, J.N., Kranz, D.M., Jameson, D.M., and Voss, Jr., E.W. (1986) Thermodynamic properties of ligand binding by monoclonal anti-fluorescyl antibodies. Biochemistry 25, 4602-4609
    • (1986) Biochemistry , vol.25 , pp. 4602-4609
    • Herron, J.N.1    Kranz, D.M.2    Jameson, D.M.3    Voss Jr., E.W.4
  • 13
    • 0000866128 scopus 로고
    • Hydrophobic effect in protein folding and other noncovalent processes involving proteins
    • Spolar, R.S., Ha, J.-H., and Record, Jr., M.T. (1989) Hydrophobic effect in protein folding and other noncovalent processes involving proteins. Proc. Natl. Acad. Sci. USA 86, 8382-8385
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8382-8385
    • Spolar, R.S.1    Ha, J.-H.2    Record Jr., M.T.3
  • 15
    • 0028280409 scopus 로고
    • Isothermal titration calorimetric study of the association of hen egg lysozyme and the anti-lysozyme antibody HyHEL-5
    • Hibbits, K.A., Gill, D.S., and Willson, R.C. (1994) Isothermal titration calorimetric study of the association of hen egg lysozyme and the anti-lysozyme antibody HyHEL-5. Biochemistry 33, 3584-3590
    • (1994) Biochemistry , vol.33 , pp. 3584-3590
    • Hibbits, K.A.1    Gill, D.S.2    Willson, R.C.3
  • 16
    • 0028999195 scopus 로고
    • Mutations in the CDRs do not cause differences in free energy during the process of formation of an activated complex between antibody and protein antigen
    • Ito, W., Yasui, H., and Kurosawa, Y. (1995) Mutations in the CDRs do not cause differences in free energy during the process of formation of an activated complex between antibody and protein antigen. J. Mol. Biol. 248, 729-732
    • (1995) J. Mol. Biol. , vol.248 , pp. 729-732
    • Ito, W.1    Yasui, H.2    Kurosawa, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.