Statistical Analysis of Protein Folding Kinetics

  1. Richard A. Friesner
  1. Aaron R. Dinner1,
  2. Sung-Sau So2,
  3. Martin Karplus3,4,5

Published Online: 13 MAR 2002

DOI: 10.1002/0471224421.ch1

Computational Methods for Protein Folding, Volume 120

Computational Methods for Protein Folding, Volume 120

How to Cite

Dinner, A. R., So, S.-S. and Karplus, M. (2002) Statistical Analysis of Protein Folding Kinetics, in Computational Methods for Protein Folding, Volume 120 (ed R. A. Friesner), John Wiley & Sons, Inc., New York, USA. doi: 10.1002/0471224421.ch1

Editor Information

  1. Columbia University, New York, New York, USA

Author Information

  1. 1

    New Chemistry Laboratory, University of Oxford, Oxford, U.K.

  2. 2

    Hoffmann-La Roche Inc., Discovery Chemistry, Nutley, NJ, U.S.A.

  3. 3

    New Chemistry Laboratory, University of Oxford, Oxford, U.K.

  4. 4

    Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA, U.S.A.

  5. 5

    Laboratoire de Chimie Biophysique, Institut le Bel, Université Louis Pasteur, Strasbourg, France

Publication History

  1. Published Online: 13 MAR 2002
  2. Published Print: 4 JAN 2002

Book Series:

  1. Advances in Chemical Physics

Book Series Editors:

  1. I. Prigogine7,8,
  2. Stuart A. Rice9

Series Editor Information

  1. 7

    Center for Studies in Statistical Mechanics and Complex Systems, The University of Texas, Austin, Texas, USA

  2. 8

    International Solvay Institutes, Université Libre de Bruxelles, Brussels, Belgium

  3. 9

    Department of Chemistry and The James Franck Institute, The University of Chicago, Chicago, Illinois, USA

ISBN Information

Print ISBN: 9780471209553

Online ISBN: 9780471224426

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Keywords:

  • proteins;
  • statistical methods;
  • lattice models;
  • folding rates;
  • unfolding rates;
  • homologous proteins

Summary

In recent years, an increasing number of proteins that lack significantly populated folding intermediates and thus exhibit two-state folding kinetics have been identified, and a range of data have been tabulated for them. The initial linear analyses of such proteins indicated that their folding rates are determined primarily by their native structures. More recently, a nonlinear, multiple-descriptor approach revealed that there is a significant dependence on the stability as well. These and related studies are discussed in Section IV.A, after an overview of the statistical methods employed in this area (Section II) and a review of the results from lattice models (Section III). An in-depth analysis of a database of 33 proteins that fold with two- or weakly three-state kinetics is presented in Sections IV.B through V. The relation of the statistical results to experiments and the model studies is discussed in Sections VI and VII.