title: Piezoelectric allostery of protein.
abstract: Allostery is indispensable for a protein to work, where a locally applied stimulus is transmitted to a distant part of the molecule. While the allostery due to chemical stimuli such as ligand binding has long been studied, the growing interest in mechanobiology prompts the study of the mechanically stimulated allostery, the physical mechanism of which has not been established. By molecular dynamics simulation of a motor protein myosin, we found that a locally applied mechanical stimulus induces electrostatic potential change at distant regions, just like the piezoelectricity. This novel allosteric mechanism, "piezoelectric allostery", should be of particularly high value for mechanosensor/transducer proteins.
authors: Department of Pure and Applied Physics, Waseda University, Tokyo 169-8555, Japan.
authors: Jun
authors: J
authors: Ohnuki
authors: Department of Pure and Applied Physics, Waseda University, Tokyo 169-8555, Japan.
authors: Takato
authors: T
authors: Sato
authors: Department of Pure and Applied Physics, Waseda University, Tokyo 169-8555, Japan.
authors: Mitsunori
authors: M
authors: Takano
mesh_terms: D000494:Allosteric Regulation; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D055672:Static Electricity
chemical_list: D011506:Proteins