Optimal specificity and function for flexible biomolecular recognition.
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.
Wang
Jin
J
State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin, People's Republic of China.
Xu
Li
L
Wang
Erkwang
E
D000596:Amino Acids / Q000737:chemistry*; D001665:Binding Sites; D001704:Biopolymers / Q000737:chemistry*; D003198:Computer Simulation; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D008958:Models, Molecular; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*
D000596:Amino Acids; D001704:Biopolymers; D011506:Proteins