How the folding rate constant of simple, single-domain proteins depends on the number of native contacts
Open Access
- 19 March 2002
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 99 (6) , 3535-3539
- https://doi.org/10.1073/pnas.052713599
Abstract
Experiments have shown that the folding rate constants of two dozen structurally unrelated, small, single-domain proteins can be expressed in terms of one quantity (the contact order) that depends exclusively on the topology of the folded state. Such dependence is unique in chemical kinetics. Here we investigate its physical origin and derive the approximate formula ln( k ) = ln( N ) + a + bN , were N is the number of contacts in the folded state, and a and b are constants whose physical meaning is understood. This formula fits well the experimentally determined folding rate constants of the 24 proteins, with single values for a and b .Keywords
This publication has 29 references indexed in Scilit:
- Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: application of long-range order to folding rate prediction11Edited by P. E. WrightJournal of Molecular Biology, 2001
- Fast Kinetics and Mechanisms in Protein FoldingAnnual Review of Biophysics, 2000
- First principles prediction of protein folding rates 1 1Edited by F. E. CohenJournal of Molecular Biology, 1999
- Deciphering the timescales and mechanisms of protein folding using minimal off-lattice modelsCurrent Opinion in Structural Biology, 1999
- Exploring structures in protein folding funnels with free energy functionals: the denatured ensembleJournal of Molecular Biology, 1999
- Protein folding: Think globally, (inter)act locallyCurrent Biology, 1998
- Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- THEORY OF PROTEIN FOLDING: The Energy Landscape PerspectiveAnnual Review of Physical Chemistry, 1997
- Rate of Intrachain Diffusion of Unfolded Cytochrome cThe Journal of Physical Chemistry B, 1997
- Theory of Elastic Mechanisms in Fibrous ProteinsJournal of the American Chemical Society, 1956