Probing the local conformational flexibility in receptor recognition: mechanistic insight from an atomic-scale investigation

摘要: Inherent protein conformational flexibility is important for biomolecular recognition, but this critical property often neglected in several studies. This event can lead to large deviations the research results. In current contribution, we disclose effects of local on receptor recognition by using an atomic-scale computational method. The results indicated that both static and dynamic reaction modes have noticeable differences, these originated from structural features molecules. Dynamic interaction displayed stability proteins had a significant influence processes. point related closely characteristics flexible loop regions where bixin located within structures. energy decomposition analyses circular dichroism validated rationality More importantly, changes some residues around binding domain were found be vital biological reactions. These microscopic findings clarified nature phenomenon could intervene recognition. Obviously, report may provide biophysical evidence exploration structure–function relationships receptors human body.