E. Trizac 1, Y. Levy 2, P. G. Wolynes 3
Proceeding of the national academy of sciences 107 (2010) 2746
Biomolecular folding and function are often coupled. During molecular recognition events, one of the binding partners may transiently or partially unfold, allowing more rapid access to a binding site. We describe a simple model for this flycasting mechanism based on the capillarity approximation and polymer chain statistics. The model shows that flycasting is most effective when the protein unfolding barrier is small and the part of the chain which extends towards the target is relatively rigid. These features are often seen in known examples of flycasting in protein-DNA binding. Simulations of protein-DNA binding based on well-funneled native-topology models with electrostatic forces confirm the trends of the analytical theory.
- 1. Laboratoire de Physique Théorique et Modèles Statistiques (LPTMS),
CNRS : UMR8626 – Université Paris XI – Paris Sud
- 2. Department of Structural Biology,
- 3. Department of Chemistry and Biochemistry,
University of California at San Diego