Adaptability of protein structures to enable functional interactions and evolutionary implications

摘要: Several studies in recent years have drawn attention to the ability of proteins adapt intermolecular interactions by conformational changes along structure-encoded collective modes motions. These so-called soft modes, primarily driven entropic effects, facilitate, if not enable, functional interactions. They represent excursions on space principal low-ascent directions/paths away from original free energy minimum, and they are accessible protein even before protein-protein/ligand An emerging concept these is evolution structures or modular domains favor such motion that will be recruited integrated for enabling Structural dynamics, including allosteric switches conformation often stabilized upon formation complexes multimeric assemblies, emerge as key properties evolutionarily maintained accomplish biological activities, consistent with paradigm sequence→structure→dynamics→function where 'dynamics' bridges structure function.