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Volumn 13, Issue 1, 2004, Pages 166-176

Two different proteins that compete for binding to thrombin have opposite kinetic and thermodynamic profiles

Author keywords

Amide H 2H exchange; Calorimetry; Enthalpy; Entropy; Hydration; MALDI TOF mass spectrometry; Surface plasmon resonance

Indexed keywords

ANION; MONOCLONAL ANTIBODY; THROMBIN; THROMBOMODULIN;

EID: 0347994109     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03120604     Document Type: Article
Times cited : (40)

References (34)
  • 2
    • 0034681302 scopus 로고    scopus 로고
    • Electrostatic dependence of the thrombin-thrombomodulin interaction
    • Baerga-Ortiz, A., Rezaie, A.R., and Komives, E.A. 2000. Electrostatic dependence of the thrombin-thrombomodulin interaction. J. Mol. Biol. 296: 651-658.
    • (2000) J. Mol. Biol. , vol.296 , pp. 651-658
    • Baerga-Ortiz, A.1    Rezaie, A.R.2    Komives, E.A.3
  • 3
    • 0036102156 scopus 로고    scopus 로고
    • Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein
    • Baerga-Ortiz, A., Hughes, C.A., Mandell, J.G., and Komives, E.A. 2002. Epitope mapping of a monoclonal antibody against human thrombin by H/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein. Protein Sci. 11: 1300-1308.
    • (2002) Protein Sci. , vol.11 , pp. 1300-1308
    • Baerga-Ortiz, A.1    Hughes, C.A.2    Mandell, J.G.3    Komives, E.A.4
  • 4
    • 0031547981 scopus 로고    scopus 로고
    • Dissecting the energetics of a protein-protein interaction: The binding of ovomucoid third domain to elastase
    • Baker, B.M. and Murphy, K.P. 1997. Dissecting the energetics of a protein-protein interaction: The binding of ovomucoid third domain to elastase. J. Mol. Biol. 268: 557-569.
    • (1997) J. Mol. Biol. , vol.268 , pp. 557-569
    • Baker, B.M.1    Murphy, K.P.2
  • 5
    • 0031030835 scopus 로고    scopus 로고
    • Energetics of cyclic dipeptide crystal packing and solvation
    • Brady, G.P. and Sharp, K.A. 1997a. Energetics of cyclic dipeptide crystal packing and solvation. Biophys. J. 72: 913-927.
    • (1997) Biophys. J. , vol.72 , pp. 913-927
    • Brady, G.P.1    Sharp, K.A.2
  • 6
    • 0030961726 scopus 로고    scopus 로고
    • Entropy in protein folding and in protein-protein interactions
    • - 1997b. Entropy in protein folding and in protein-protein interactions. Curr. Opin. Struct. Biol. 7: 215-221.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 215-221
  • 7
    • 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
  • 8
    • 0021704088 scopus 로고
    • Monoclonal antibodies directed against human α-thrombin and the thrombinantithrombin III complex
    • Dawes, J., James, K., Micklem, L., Pepper, D., and Prowse, C. 1984. Monoclonal antibodies directed against human α-thrombin and the thrombinantithrombin III complex. Thromb. Res. 36: 397-409.
    • (1984) Thromb. Res. , vol.36 , pp. 397-409
    • Dawes, J.1    James, K.2    Micklem, L.3    Pepper, D.4    Prowse, C.5
  • 9
    • 0036228119 scopus 로고    scopus 로고
    • Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface- and solution-based biophysical methods
    • Day, Y.S., Baird, C.L., Rich, R.L., and Myszka, D.G, 2002. Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface- and solution-based biophysical methods. Protein Sci. 11: 1017-1025.
    • (2002) Protein Sci. , vol.11 , pp. 1017-1025
    • Day, Y.S.1    Baird, C.L.2    Rich, R.L.3    Myszka, D.G.4
  • 10
    • 0029112841 scopus 로고
    • Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface
    • Esmon, C.T. 1995. Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface. FASEB J. 9: 946-955.
    • (1995) FASEB J. , vol.9 , pp. 946-955
    • Esmon, C.T.1
  • 12
    • 0034651984 scopus 로고    scopus 로고
    • Water penetration and escape in proteins
    • Garcia, A.E. and Hummer, G. 2000. Water penetration and escape in proteins. Proteins 38: 261-272.
    • (2000) Proteins , vol.38 , pp. 261-272
    • Garcia, A.E.1    Hummer, G.2
  • 13
    • 0029941271 scopus 로고    scopus 로고
    • Energetics of hydrogen bonding in proteins: A model compound study
    • Habermann, S.M. and Murphy, K.P. 1996. Energetics of hydrogen bonding in proteins: A model compound study. Protein Sci. 5: 1229-1239.
    • (1996) Protein Sci. , vol.5 , pp. 1229-1239
    • Habermann, S.M.1    Murphy, K.P.2
  • 14
    • 0031010107 scopus 로고    scopus 로고
    • The kinetics of protein-protein recognition
    • Janin, J. 1997. The kinetics of protein-protein recognition. Proteins 28: 153-161.
    • (1997) Proteins , vol.28 , pp. 153-161
    • Janin, J.1
  • 15
    • 0030266484 scopus 로고    scopus 로고
    • Sensing the heat: The application of isothermal titration calorimetry to thermodynamic studies of biomolecular interactions
    • Ladbury, J.E. and Chowdhry, B.Z. 1996. Sensing the heat: The application of isothermal titration calorimetry to thermodynamic studies of biomolecular interactions. Chem. Biol. 3: 791-801.
    • (1996) Chem. Biol. , vol.3 , pp. 791-801
    • Ladbury, J.E.1    Chowdhry, B.Z.2
  • 17
    • 0032428378 scopus 로고    scopus 로고
    • Identification of protein-protein interfaces by decreased amide proton solvent accessibility
    • Mandell, J.G., Falick, A.M., and Komives, E.A. 1998a. Identification of protein-protein interfaces by decreased amide proton solvent accessibility. Proc. Natl. Acad. Sci. 95: 14705-14710.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 14705-14710
    • Mandell, J.G.1    Falick, A.M.2    Komives, E.A.3
  • 18
    • 0032186122 scopus 로고    scopus 로고
    • Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry
    • -. 1998b. Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry. Anal. Chem. 70: 3987-3995.
    • (1998) Anal. Chem. , vol.70 , pp. 3987-3995
  • 20
    • 0027537127 scopus 로고
    • Structural energetics of peptide recognition: Angiotensin II/antibody binding
    • Murphy, K.P., Xie, D., Garcia, K.C., Amzel, L.M., and Freire, E. 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
  • 21
    • 0025338124 scopus 로고
    • Thrombin-bound conformation of the C-terminal fragments of hirudin determined by transferred nuclear Overhauser effects
    • Ni, F., Konishi, Y., and Scheraga, H.A. 1990. Thrombin-bound conformation of the C-terminal fragments of hirudin determined by transferred nuclear Overhauser effects. Biochemistry 29: 4479-4489.
    • (1990) Biochemistry , vol.29 , pp. 4479-4489
    • Ni, F.1    Konishi, Y.2    Scheraga, H.A.3
  • 22
    • 0032720338 scopus 로고    scopus 로고
    • Isothermal titration calorimetry of protein-protein interactions
    • Pierce, M.M., Raman, C.S., and Nall, B.T. 1999. Isothermal titration calorimetry of protein-protein interactions. Methods 19: 213-221.
    • (1999) Methods , vol.19 , pp. 213-221
    • Pierce, M.M.1    Raman, C.S.2    Nall, B.T.3
  • 23
    • 0041009405 scopus 로고    scopus 로고
    • Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes
    • Shick, K.A., Xavier, K.A., Rajpal, A., Smith-Gill, S.J., and Willson, R.C. 1997. Association of the anti-hen egg lysozyme antibody HyHEL-5 with avian species variant and mutant lysozymes. Biochim. Biophys. Acta 1340: 205-214.
    • (1997) Biochim. Biophys. Acta , vol.1340 , pp. 205-214
    • Shick, K.A.1    Xavier, K.A.2    Rajpal, A.3    Smith-Gill, S.J.4    Willson, R.C.5
  • 24
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker, B.A., Portman, J.J., and Wolynes, P.G. 2000. Speeding molecular recognition by using the folding funnel: The fly-casting mechanism. Proc. Natl. Acad. Sci. 97: 8868-8873.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 25
    • 0033615637 scopus 로고    scopus 로고
    • Thermodynamic analyses reveal role of water release in epitope recognition by a monoclonal antibody against the human guanylyl cyclase C receptor
    • Swaminathan, C.P., Nandi, A., Visweswariah, S.S., and Surolia, A. 1999. Thermodynamic analyses reveal role of water release in epitope recognition by a monoclonal antibody against the human guanylyl cyclase C receptor. J. Biol. Chem. 274: 31272-31278.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31272-31278
    • Swaminathan, C.P.1    Nandi, A.2    Visweswariah, S.S.3    Surolia, A.4
  • 26
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai, C.J., Kumar, S., Ma, B., and Nussinov, R. 1999. Folding funnels, binding funnels, and protein function. Protein Sci. 8: 1181-1190.
    • (1999) Protein Sci. , vol.8 , pp. 1181-1190
    • Tsai, C.J.1    Kumar, S.2    Ma, B.3    Nussinov, R.4
  • 27
    • 0030948651 scopus 로고    scopus 로고
    • Energetics of thrombin-thrombomodulin interaction
    • Vindigni, A., White, C.E., Komives, E.A., and Di Cera, E. 1997. Energetics of thrombin-thrombomodulin interaction. Biochemistry 36: 6674-6681.
    • (1997) Biochemistry , vol.36 , pp. 6674-6681
    • Vindigni, A.1    White, C.E.2    Komives, E.A.3    Di Cera, E.4
  • 28
    • 0029586382 scopus 로고
    • Large-scale expression, purification and characterization of small fragments of thrombomodulin: The roles of the sixth domain and of methionine 388
    • White, C.E., Hunter, M.J., Meininger, D.P., White, L.R., and Komives, E.A. 1995. Large-scale expression, purification and characterization of small fragments of thrombomodulin: The roles of the sixth domain and of methionine 388. Protein Eng. 8: 1177-1187.
    • (1995) Protein Eng. , vol.8 , pp. 1177-1187
    • White, C.E.1    Hunter, M.J.2    Meininger, D.P.3    White, L.R.4    Komives, E.A.5
  • 29
    • 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
  • 30
    • 0032587512 scopus 로고    scopus 로고
    • Production of large quantities of isotopically labeled protein in Pichia pastoris by fermentation
    • Wood, M.J. and Komives, E.A. 1999. Production of large quantities of isotopically labeled protein in Pichia pastoris by fermentation. J. Biomol. NMR 13: 149-159.
    • (1999) J. Biomol. NMR , vol.13 , pp. 149-159
    • Wood, M.J.1    Komives, E.A.2
  • 31
    • 0034006172 scopus 로고    scopus 로고
    • Solution structure of the smallest cofactor-active fragment of thrombomodulin
    • Wood, M.J., Sampoli-Benitez, B.A., and Komives, E.A. 2000. Solution structure of the smallest cofactor-active fragment of thrombomodulin. Nat. Struct. Biol. 7: 200-204.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 200-204
    • Wood, M.J.1    Sampoli-Benitez, B.A.2    Komives, E.A.3
  • 32
    • 0030770571 scopus 로고    scopus 로고
    • Involvement of water molecules in the association of monoclonal antibody Hy-HEL-5 with bobwhite quail lysozyme
    • Xavier, K.A., Shick, K.A., Smith-Gill, S.J., and Willson, R.C. 1997. Involvement of water molecules in the association of monoclonal antibody Hy-HEL-5 with bobwhite quail lysozyme. Biophys. J. 73: 2116-2125.
    • (1997) Biophys. J. , vol.73 , pp. 2116-2125
    • Xavier, K.A.1    Shick, K.A.2    Smith-Gill, S.J.3    Willson, R.C.4
  • 33
    • 0031106828 scopus 로고    scopus 로고
    • Thermodynamic analysis of antigen-antibody binding using biosensor measurements at different temperatures
    • Zeder-Lutz, G., Zuber, E., Witz, J., and Van Regenmortel, M.H. 1997. Thermodynamic analysis of antigen-antibody binding using biosensor measurements at different temperatures. Anal. Biochem. 246: 123-132.
    • (1997) Anal. Biochem. , vol.246 , pp. 123-132
    • Zeder-Lutz, G.1    Zuber, E.2    Witz, J.3    Van Regenmortel, M.H.4
  • 34
    • 0032710610 scopus 로고    scopus 로고
    • Increased protein backbone conformational entropy upon hydrophobic ligand binding
    • Zídek, L., Novotny, M.V., and Stone, M.J. 1999. Increased protein backbone conformational entropy upon hydrophobic ligand binding. Nat. Struct. Biol. 6: 1118-1121.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1118-1121
    • Zídek, L.1    Novotny, M.V.2    Stone, M.J.3


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