Protein binding dynamics:

Recent advances on our understanding of protein binding has shown that the onset of this process is not the fully desolvated interface, dominated by van der Waals interactions, but instead a smoother landscape governed by the the long-range (10 A) electrostatics and intermediate-range (5 A) solvation forces between molecules. These forces, which provide the initial attraction between ligands and their receptors, were also found consistent with a relatively narrow docking pathway to the final bound conformation. On the other hand, it is well known that surface complementarity, led by short-range vdW forces, play a crucial role on the stability and specificity of the high affinity complex. These properties indicate that the intrinsic dynamic nature of protein binding leads to distinct kinetic regimes where different driving forces with diverse length scales governed the binding process at different times. [1]|[2]|[3]