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Optimal Specificity and Function for Flexible Biomolecular Recognition

Jin Wang ^* , Li Xu ^* and Erkwang Wang ^*

^* State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin, People's Republic of China; and Department of Chemistry and Department of Physics, State University of New York at Stony Brook, Stony Brook, New York

Correspondence: Address reprint requests and inquiries to Jin Wang, E-mail: jin.wang.1{at}stonybrook.edu; or Erkang Wang, E-mail: ekwang{at}ciac.jl.cn.

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.

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