Small Molecule Binding to Proteins: Affinity and Binding/Unbinding Dynamics from Atomistic Simulations

Abstract

A dynamic situation! Molecular dynamics simulations at equilibrium are shown to correctly identify the binding mode of dimethyl sulfoxide in the rotamase FKBP without using any experimental information or bias. Furthermore, both the binding and unbinding kinetics were found to have a double-exponential time dependence. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.