Insights into Specific Problems in Protein Folding Using Simple Concepts
- Richard A. Friesner
Published Online: 13 MAR 2002
DOI: 10.1002/0471224421.ch2
Copyright © 2002 John Wiley & Sons, Inc.
Book Title
Computational Methods for Protein Folding, Volume 120
Additional Information
How to Cite
Thirumalai, D., Klimov, D. K. and Dima, R. I. (2002) Insights into Specific Problems in Protein Folding Using Simple Concepts, in Computational Methods for Protein Folding, Volume 120 (ed R. A. Friesner), John Wiley & Sons, Inc., New York, USA. doi: 10.1002/0471224421.ch2
Editor Information
Columbia University, New York, New York, USA
Publication History
- Published Online: 13 MAR 2002
- Published Print: 4 JAN 2002
Book Series:
Book Series Editors:
- I. Prigogine3,4,
- Stuart A. Rice5
Series Editor Information
- 3
Center for Studies in Statistical Mechanics and Complex Systems, The University of Texas, Austin, Texas, USA
- 4
International Solvay Institutes, Université Libre de Bruxelles, Brussels, Belgium
- 5
Department of Chemistry and The James Franck Institute, The University of Chicago, Chicago, Illinois, USA
ISBN Information
Print ISBN: 9780471209553
Online ISBN: 9780471224426
- Summary
- Chapter
Keywords:
- proteins;
- lattice representations;
- conformational space;
- dense sequence space;
- protein folding;
- disulfide bonds;
- chaperonin-facilitated protein folding
Summary
The purpose of this chapter is to describe applications of simple concepts and computations to three specific problems in protein folding: (i) Are the requirements that folded states of proteins be compact and have low energy sufficient to explain the emergence of the finite number of folds from a very dense sequence space? (ii) Phenomenological theory and lattice model computations are used to clarify the role of disulfide bonds in protein folding. (iii) A simple model of chaperonin-assisted folding is described.
The authors briefly describe lattice models and the commonly employed computational methods. This is followed by a brief description of how a monomeric protein folds. The chapter concludes with brief comments about the challenges we face in the straightforward all-atom simulations of protein folding.