Efficient incorporation of protein flexibility and dynamics into molecular docking simulations

摘要

Flexibility and dynamics are protein characteristics that are essential for the process of molecular recognition. Conformational changes in the protein that are coupled to ligand binding are described by the biophysical models of induced fit and conformational selection. Different concepts are reviewed that incorporate protein flexibility into protein-ligand docking within the context of these two models. Several computational studies will be presented that discuss the validity and possible limitations of such approaches. Finally, different approaches that incorporate protein dynamics, e.g. configurational entropy, and solvation effects into docking will be highlighted.