Optimal specificity and function for flexible biomolecular recognition

Biophys J. 2007 Jun 15;92(12):L109-11. doi: 10.1529/biophysj.107.105551. Epub 2007 Apr 6.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / chemistry*
  • Binding Sites*
  • Biopolymers / chemistry*
  • Computer Simulation
  • Hydrophobic and Hydrophilic Interactions
  • Models, Chemical*
  • Models, Molecular*
  • Protein Binding*
  • Proteins / chemistry*

Substances

  • Amino Acids
  • Biopolymers
  • Proteins