Sorting Perturbed Proteins

摘要

Allostery is a universal phenomenon: all dynamic proteins are potentially allosteric. Crucial in all cellular pathways, it comes about when a perturbation by a molecule called an effector alters a protein's shape and/or dynamics and leads to a functional change at the substrate binding site. Allosteric perturbation can arise due to small or large molecule binding; changesrnin pH, temperature, ionic strength, or concentration; or fromrncovalent modifications such as sugar or phosphoryl group linking. Yet, despite how much we know about how allostery occurs, how signals initiating at a perturbation site transmit through a protein is still anrnopen question.