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Volumn 25, Issue 8, 2011, Pages 2804-2813

Temperature dependence of internal friction in enzyme reactions

Author keywords

Kramers' theory; Rough energy landscape; Trypsin activation

Indexed keywords

TRYPSIN;

EID: 80051679031     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.11-180794     Document Type: Article
Times cited : (13)

References (32)
  • 1
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • Kramers, H. A. (1940) Brownian motion in a field of force and the diffusion model of chemical reactions. Physica 7, 284-304
    • (1940) Physica , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 2
    • 0347193736 scopus 로고
    • Reaction-rate theory: Fifty years after Kramers
    • Hänggi, P., Talkner, P., and Borkovec, M. (1990) Reaction-rate theory: fifty years after Kramers. Rev. Mod. Phys. 62, 251-342
    • (1990) Rev. Mod. Phys. , vol.62 , pp. 251-342
    • Hänggi, P.1    Talkner, P.2    Borkovec, M.3
  • 3
    • 0026636807 scopus 로고
    • The role of solvent viscosity in the dynamics of protein conformational changes
    • Ansari, A., Jones, C. M., Henry, E. R., Hofrichter, J., and Eaton, W. A. (1992) The role of solvent viscosity in the dynamics of protein conformational changes. Science 256, 1796-1798
    • (1992) Science , vol.256 , pp. 1796-1798
    • Ansari, A.1    Jones, C.M.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.A.5
  • 4
    • 0028271936 scopus 로고
    • Conformational relaxation and ligand binding in myoglobin
    • DOI 10.1021/bi00183a017
    • Ansari, A., Jones, C. M., Henry, E. R., Hofrichter, J., and Eaton, W. A. (1994) Conformational relaxation and ligand binding in myoglobin. Biochemistry 33, 5128-5145 (Pubitemid 24150979)
    • (1994) Biochemistry , vol.33 , Issue.17 , pp. 5128-5145
    • Ansari, A.1    Jones, C.M.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.A.5
  • 5
    • 0035797991 scopus 로고    scopus 로고
    • Origin of friction derived from rupture dynamics
    • Suda, H. (2001) Origin of friction derived from rupture dynamics. Langmuir 17, 6045
    • (2001) Langmuir , vol.17 , pp. 6045
    • Suda, H.1
  • 7
    • 73249133356 scopus 로고    scopus 로고
    • Direct observation of ultrafast folding and denatured state dynamics in single protein molecules
    • Neuweiler, H., Johnson, C. M., and Fersht, A. R. (2009) Direct observation of ultrafast folding and denatured state dynamics in single protein molecules. Proc. Natl. Acad. Sci. U. S. A. 106, 18569-18574
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 18569-18574
    • Neuweiler, H.1    Johnson, C.M.2    Fersht, A.R.3
  • 8
    • 4744357562 scopus 로고    scopus 로고
    • Internal friction controls the speed of protein folding from a compact configuration
    • DOI 10.1021/bi048822m
    • Pabit, S. A., Roder, H., and Hagen, S. J. (2004) Internal friction controls the speed of protein folding from a compact configuration. Biochemistry 43, 12532-12538 (Pubitemid 39314714)
    • (2004) Biochemistry , vol.43 , Issue.39 , pp. 12532-12538
    • Pabit, S.A.1    Roder, H.2    Hagen, S.J.3
  • 10
    • 1642379707 scopus 로고    scopus 로고
    • A Limiting Speed for Protein Folding at Low Solvent Viscosity
    • DOI 10.1021/ja049966r
    • Qiu, L., and Hagen, S. J. (2004) A limiting speed for protein folding at low solvent viscosity. J. Am. Chem. Soc. 126, 3398-3399 (Pubitemid 38366711)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.11 , pp. 3398-3399
    • Qiu, L.1    Hagen, S.J.2
  • 11
    • 34248594515 scopus 로고    scopus 로고
    • Site directed mutagenesis at position 193 of human trypsin 4 alters the rate of conformational change during activation: Role of local internal viscosity in protein dynamics
    • DOI 10.1002/prot.21398
    • Toth, J., Simon, Z., Medveczky, P., Gombos, L., Jelinek, B., Szilagyi, L., Graf, L., and Malnasi-Csizmadia, A. (2007) Site directed mutagenesis at position 193 of human trypsin 4 alters the rate of conformational change during activation: role of local internal viscosity in protein dynamics. Proteins 67, 1119-1127 (Pubitemid 46753956)
    • (2007) Proteins: Structure, Function and Genetics , vol.67 , Issue.4 , pp. 1119-1127
    • Toth, J.1    Simon, Z.2    Medveczky, P.3    Gombos, L.4    Jelinek, B.5    Szilagyi, L.6    Graf, L.7    Malnasi-Csizmadia, A.8
  • 12
    • 0015994917 scopus 로고
    • PH dependence of chymotrypsin catalysis. Appendix: Substrate binding to dimeric alpha-chymotrypsin studied by x-ray diffraction and the equilibrium method
    • Fersht, A. R., and Renard, M. (1974) pH dependence of chymotrypsin catalysis. Appendix: substrate binding to dimeric alpha-chymotrypsin studied by x-ray diffraction and the equilibrium method. Biochemistry 13, 1416-1426
    • (1974) Biochemistry , vol.13 , pp. 1416-1426
    • Fersht, A.R.1    Renard, M.2
  • 13
    • 0024350344 scopus 로고
    • Raman spectroscopic study of the changes in secondary structure of chymotrypsin: Effect of pH and pressure on the salt bridge
    • DOI 10.1016/0167-4838(89)90217-3
    • Heremans, L., and Heremans, K. (1989) Raman spectroscopic study of the changes in secondary structure of chymotrypsin: effect of pH and pressure on the salt bridge. Biochim. Biophys. Acta 999, 192-197 (Pubitemid 20000179)
    • (1989) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.999 , Issue.2 , pp. 192-197
    • Heremans, L.1    Heremans, K.2
  • 14
    • 0018133246 scopus 로고
    • Refolding transition of alpha-chymotrypsin: pH and salt dependence
    • Stoesz, J. D., and Lumry, R. W. (1978) Refolding transition of alpha-chymotrypsin: pH and salt dependence. Biochemistry 17, 3693-3699 (Pubitemid 9022575)
    • (1978) Biochemistry , vol.17 , Issue.18 , pp. 3693-3699
    • Stoesz, J.D.1    Lumry, R.W.2
  • 15
    • 4344569109 scopus 로고    scopus 로고
    • A fluorescence stopped-flow kinetic study of the conformational activation of alpha-chymotrypsin and several mutants
    • DOI 10.1110/ps.04709604
    • Verheyden, G., Matrai, J., Volckaert, G., and Engelborghs, Y. (2004) A fluorescence stopped-flow kinetic study of the conformational activation of alpha-chymotrypsin and several mutants. Protein Sci. 13, 2533-2540 (Pubitemid 39128874)
    • (2004) Protein Science , vol.13 , Issue.9 , pp. 2533-2540
    • Verheyden, G.1    Matrai, J.2    Volckaert, G.3    Engelborghs, Y.4
  • 16
    • 0017893796 scopus 로고
    • The transition of bovine trypsinogen to a trypsin like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution
    • Bode, W., Schwager, P., and Huber, R. (1978) The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen- pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution. J. Mol. Biol. 118, 99-112 (Pubitemid 8271375)
    • (1978) Journal of Molecular Biology , vol.118 , Issue.1 , pp. 99-112
    • Bode, W.1    Schwager, P.2    Huber, R.3
  • 17
    • 38949084592 scopus 로고    scopus 로고
    • Probing conformational plasticity of the activation domain of trypsin: The role of glycine hinges
    • DOI 10.1021/bi701454e
    • Gombos, L., Kardos, J., Patthy, A., Medveczky, P., Szilagyi, L., Malnasi-Csizmadia, A., and Graf, L. (2008) Probing conformational plasticity of the activation domain of trypsin: the role of glycine hinges. Biochemistry 47, 1675-1684 (Pubitemid 351231217)
    • (2008) Biochemistry , vol.47 , Issue.6 , pp. 1675-1684
    • Gombos, L.1    Kardos, J.2    Patthy, A.3    Medveczky, P.4    Szilagyi, L.5    Malnasi-Csizmadia, A.6    Graf, L.7
  • 18
    • 21844455282 scopus 로고    scopus 로고
    • Energetic and structural consequences of perturbing Gly-193 in the oxyanion hole of serine proteases
    • DOI 10.1074/jbc.M503499200
    • Bobofchak, K. M., Pineda, A. O., Mathews, F. S., and Di Cera, E. (2005) Energetic and structural consequences of perturbing Gly-193 in the oxyanion hole of serine proteases. J. Biol. Chem. 280, 25644-25650 (Pubitemid 40962273)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.27 , pp. 25644-25650
    • Bobofchak, K.M.1    Pineda, A.O.2    Mathews, F.S.3    Di, C.E.4
  • 19
    • 0036304291 scopus 로고    scopus 로고
    • Crystal structure reveals basis for the inhibitor resistance of human brain trypsin
    • DOI 10.1006/jmbi.2001.5305
    • Katona, G., Berglund, G. I., Hajdu, J., Graf, L., and Szilagyi, L. (2002) Crystal structure reveals basis for the inhibitor resistance of human brain trypsin. J. Mol. Biol. 315, 1209-1218 (Pubitemid 34729298)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.5 , pp. 1209-1218
    • Katona, G.1    Berglund, G.I.2    Hajdu, J.3    Graf, L.4    Szilagyi, L.5
  • 20
    • 0034613031 scopus 로고    scopus 로고
    • C,T-Dependence of the viscosity and the self-diffusion coefficients in some aqueous carbohydrate solutions
    • Rampp, M., Buttersack, C., and Lüdemann, H.-D. (2000) c,T-Dependence of the viscosity and the self-diffusion coefficients in some aqueous carbohydrate solutions. Carb. Res. 328, 561
    • (2000) Carb. Res. , vol.328 , pp. 561
    • Rampp, M.1    Buttersack, C.2    Lüdemann, H.-D.3
  • 21
    • 33744948792 scopus 로고    scopus 로고
    • Thermodynamic analysis reveals structural rearrangement during the acylation step in human trypsin 4 on 4-methylumbelliferyl 4-guanidinobenzoate substrate analogue
    • DOI 10.1074/jbc.M512301200
    • Toth, J., Gombos, L., Simon, Z., Medveczky, P., Szilagyi, L., Graf, L., and Malnasi-Csizmadia, A. (2006) Thermodynamic analysis reveals structural rearrangement during the acylation step in human trypsin 4 on 4-methylumbelliferyl 4-guanidinobenzoate substrate analogue. J. Biol. Chem. 281, 12596-12602 (Pubitemid 43855348)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12596-12602
    • Toth, J.1    Gombos, L.2    Simon, Z.3    Medveczky, P.4    Szilagyi, L.5    Graf, L.6    Malnasi-Csizmadia, A.7
  • 24
    • 77957916566 scopus 로고    scopus 로고
    • Solvent viscosity and friction in protein folding dynamics
    • Hagen, S. J. (2010) Solvent viscosity and friction in protein folding dynamics. Curr. Protein Pept. Sci. 11, 385-395
    • (2010) Curr. Protein Pept. Sci. , vol.11 , pp. 385-395
    • Hagen, S.J.1
  • 25
    • 0000794732 scopus 로고
    • Transient kinetics of chemical reactions with bounded diffusion perpendicular to the reaction coordinate: Intramolecular processes with slow conformational changes
    • Agmon, N., and Hopfield, J. J. (1982) Transient kinetics of chemical reactions with bounded diffusion perpendicular to the reaction coordinate: Intramolecular processes with slow conformational changes. J. Chem. Phys. 78, 6947-6959
    • (1982) J. Chem. Phys. , vol.78 , pp. 6947-6959
    • Agmon, N.1    Hopfield, J.J.2
  • 26
    • 5244325378 scopus 로고
    • Dynamical disorder: Passage through a fluctuating bottleneck
    • Zwanzig, R. (1992) Dynamical disorder: passage through a fluctuating bottleneck. J. Chem. Phys. 97, 3587-3589
    • (1992) J. Chem. Phys. , vol.97 , pp. 3587-3589
    • Zwanzig, R.1
  • 27
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., Sligar, S. G., and Wolynes, P. G. (1991) The energy landscapes and motions of proteins. Science 254, 1598-1603 (Pubitemid 21917496)
    • (1991) Science , vol.254 , Issue.5038 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 29
    • 0000076228 scopus 로고
    • Diffusion coefficient for a Brownian particle in a periodic field of force: I. Large friction limit. Phys. A Stat
    • Festa, R., and d'Agliano, E. G. (1978) Diffusion coefficient for a Brownian particle in a periodic field of force: I. Large friction limit. Phys. A Stat. Theor. Phys. 90, 229
    • (1978) Theor. Phys. , vol.90 , pp. 229
    • Festa, R.1    D'Agliano, E.G.2
  • 30
  • 32
    • 20044395620 scopus 로고    scopus 로고
    • Direct measurement of protein energy landscape roughness
    • DOI 10.1038/sj.embor.7400403
    • Nevo, R., Brumfeld, V., Kapon, R., Hinterdorfer, P., and Reich, Z. (2005) Direct measurement of protein energy landscape roughness. EMBO Rep. 6, 482-486 (Pubitemid 40767083)
    • (2005) EMBO Reports , vol.6 , Issue.5 , pp. 482-486
    • Nevo, R.1    Brumfeld, V.2    Kapon, R.3    Hinterdorfer, P.4    Reich, Z.5


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