Hostname: page-component-cd9895bd7-gvvz8 Total loading time: 0 Render date: 2025-01-06T03:36:54.105Z Has data issue: false hasContentIssue false
  • English
  • Français

Entropic barriers, transition states, funnels, and exponential protein folding kinetics: A simple model

Published online by Cambridge University Press:  01 March 2000

D.J. BICOUT  and
ATTILA SZABO
D.J. BICOUT
Affiliation:
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bldg. 5, Bethesda, Maryland 20892
ATTILA SZABO
Affiliation:
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bldg. 5, Bethesda, Maryland 20892
Get access

Abstract

This paper presents an analytically tractable model that captures the most elementary aspect of the protein folding problem, namely that both the energy and the entropy decrease as a protein folds. In this model, the system diffuses within a sphere in the presence of an attractive spherically symmetric potential. The native state is represented by a small sphere in the center, and the remaining space is identified with unfolded states. The folding temperature, the time-dependence of the populations, and the relaxation rate are calculated, and the folding dynamics is analyzed for both golf-course and funnel-like energy landscapes. This simple model allows us to illustrate a surprising number of concepts including entropic barriers, transition states, funnels, and the origin of single exponential relaxation kinetics.

Keywords

diffusionexponential kineticsfree energy barriersprotein folding
Type
Research Article
Information
Protein Science , Volume 9 , Issue 3 , March 2000 , pp. 452 - 465
Copyright
© 2000 The Protein Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)