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Biophys. J. BioFAST: First Published April 6, 2007. doi:10.1529/biophysj.107.105551
© 2007 by the Biophysical Society.

A more recent version of this article appeared on June 15, 2007.
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BIOPHYSICAL THEORY AND MODELING

Optimal Specificity and Function for Flexible Biomolecular Recognition

Jin Wang 1*, Li Xu 2 and Erkang Wang 3

1 State University of New York at Stony Brook
2 Changchun Institue of Applied Chemistry
3 Changchun Institute of Applied Chemistry

* To whom correspondence should be addressed. E-mail: jin.wang.1{at}stonybrook.edu.

Submitted on January 30, 2007
Revised on March 3, 2007
Accepted on 20 March 2007


  Abstract
Biomolecular associations often accompanied by large conformational changes, sometimes folding and unfolding. By exploring an exactly solvable model, we constructed the free energy landscape and established a general framework for studying the biomolecular flexible binding process. We derived an optimal criterion for the specificity and function for flexible biomolecular binding where the binding and conformational folding are coupled.

Key Words: Binding with Large Conformational Changes, Binding-Folding Coupling, Biomolecular Recognition, Flexible Binding, Optimal Function, Optimal Specificity






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Copyright © 2007 by the Biophysical Society.