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Biophys. J. BioFAST: First Published August 12, 2005. doi:10.1529/biophysj.105.069336
© 2005 by the Biophysical Society.

A more recent version of this article appeared on October 1, 2005.
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BIOPHYSICAL LETTERS

The Entropic Cost of Protein-Protein Association: A Case Study on Acetylcholinesterase Binding to Fasciculin-2

David D.L. Minh 1*, Jennifer M. Bui 1, Chia-en Chang 1, Tushar Jain 1, Jessica M.J. Swanson 2 and J. Andrew McCammon 2

1 University of California San Diego
2 University of California at San Diego

* To whom correspondence should be addressed. E-mail: dminh{at}mccammon.ucsd.edu.

Submitted on June 22, 2005
Revised on July 8, 2005
Accepted on 19 July 2005


  Abstract
Protein-protein association is accompanied by a large reduction in translational and rotational (external) entropy. Based on a 15 ns MD simulation of acetylcholinesterase (AChE) in complex with fasciculin 2 (Fas2), we estimate the loss in external entropy using quasiharmonic analysis and histogram-based approximations of the probability distribution function. The external entropy loss of AChE-Fas2 binding, about 30 cal/mol K, is found to be significantly larger than most previously characterized protein-ligand systems. However, it is less than the entropy loss estimated by Finkelstein and Janin (1989), which was based on atomic motions in crystals.

Key Words: complexation, entropy, free energy, protein-protein association, residual motion, translational and rotational




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Copyright © 2005 by the Biophysical Society.