Dynamics of hydrogen bond desolvation in protein folding.

摘要: Abstract As proteins fold, a progressive structuring, immobilization and eventual exclusion of water surrounding backbone hydrogen bonds takes place. This process turns into major determinants the folding pathway compensates for penalty desolvation polar groups. Taken as an average over all in native this extent protection is found to be nearly ubiquitous. It dynamically crucial, determining constraint long-time limit behavior coarse-grained ab initio simulations. Furthermore, examination one longest available (1 μs) all-atom simulations with explicit solvent reveals that constant motion trajectory. We propose how such stabilization best achieved by clustering five hydrophobes around bonds, arrangement yields optimal stabilization. Our results support clarify view hydrophobic surface burial should commensurate hydrogen-bond formation enable us define basic motif inherent structure dynamics.