Single-molecule dynamics reveals cooperative binding-folding in protein recognition.

ABSTRACT: The study of associations between two biomolecules is the key to understanding molecular function and recognition. Molecular function is often thought to be determined by underlying structures. Here, combining a single-molecule study of protein binding with an energy-landscape-inspired microscopic model, we found strong evidence that biomolecular recognition is determined by flexibilities in addition to structures. Our model is based on coarse-grained molecular dynamics on the residue level with the energy function biased toward the native binding structure (the Go model). With our model, the underlying free-energy landscape of the binding can be explored. There are two distinct conformational states at the free-energy minimum, one with partial folding of CBD itself and significant interfa

SUBMITTER: Wang J 

PROVIDER: S-EPMC1487182 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature