Importance of intramolecular protein dynamics to kinetics of biochemical processes

• Autorzy: Kurzynski M.
• Języki publikacji: EN

Abstrakty

EN

Several points seem essential for construction of the future statistical theory of biochemical processes. (a) The native proteins involved in these processes reveal a purely stochastic intramolecular dynamics of conformational transitions much slower than the usual vibrational dynamics. At least in the range from 10-11 to 10-7s the relaxation time spectrum of conformational transition dynamics is practically quasi-continuous. (b) The majority of reactions involving proteins are controlled and, presumably, also gated by this stochastic dynamics. (c) Of special importance is the short initial-condition dependent stage of biochemical reactions, neglected in the description of the reaction in terms of the standard kinetics. This stage is directly observed in experiments in which especially prepared initial conformational substates of the protein are confined to the reaction transition state. (d) The initial-condition dependent stage, and not that described by the standard kinetics, is responsible for the coupling of component reactions in the complete catalytic cycles proceeding in the steady-state and more complex processes of biological free energy transduction.

Słowa kluczowe

EN

biochemical process; enzymatic catalysis; intramolecular protein; transduction; free energy; kinetics; protein; protein dynamics

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 1999
• Tom: 04
• Numer: 1
• Opis fizyczny: p.117-130,fig.

Twórcy

autor

Kurzynski M.

• A.Mickiewicz University, Umultowska 85, 61-614 Poznan, Poland

Bibliografia

• 1. McCammon, J. A. and Harvey, S. C. Dynamics of Proteins and Nucleic Acids, Cambridge University, Cambridge, 1987.
• 2. Brooks III, C. L., Karplus, M. and Pettitt, B. M. Proteins: A Theoretical Perspective of Dynamics, Structure and Thermodynamics, Advances in Chemical Physics, vol. 71, Wiley, New York, 1988.
• 3. Frauenfelder, H., Steinbach, P. J. and Young, R. D., Chemica Scripta 29A (1989) 145-150.
• 4. Frauenfelder, H., Sligar, S. G. and Wolynes, P. G. Science 254 (1991) 1598-1603.
• 5. Kurzyński, M. Progr. Biophys. Molec. Biol. 69 (1998) 23-82.
• 6. Kurzyński, M. FEBS Lett. 328 (1993) 221-224.
• 7. Kurzyński, M. Biophys. Chem. 57 (1997) 1-28.
• 8. Stein, D. L., ed. Spin Glasses in Biology, World Scientific, Singapore, 1992.
• 9. Kurzyński, M. Acta Phys. Pol. B28 (1997) 1853-1889.
• 10. Kurzyński, M., Palacz, K. and Chełminiak, P. Proc. Natl. Acad. Sci. USA 95 (1998) 11685-11690.
• 11. Sansom, M. S. P., Ball, F. G., Kerry, C. J., McGee, R., Ramsey, R. L. and Usherwood, P. N. R. Biophys. J. 56 (1989) 1229-1243.
• 12. Kurzyński, M., Chełminiak, P. and Palacz, K. Proc. Natl. Acad. Sci. USA, submitted for publication.
• 13. Nadler, W. and Stein, D. L. Proc. Natl. Acad. Sci. USA 88 (1991) 6750-6754.
• 14. Nadler, W. and Stein, D. L. J. Chem. Phys. 104 (1996) 1918-1936.
• 15. Fersht, A. Enzyme Structure and Mechanism, 2nd edn., Freeman, New York, 1969.
• 16. Juelicher, F., Ajdari, A. and Prost, J. Revs. Mod. Phys. 69 (1997) 1269-1281.
• 17. Hill, T. L. Free Energy Transduction and Biochemical Cycle Kinetics, Springer, New York, 1989.