TY - JOUR
T1 - Piezoelectric allostery of protein
AU - Ohnuki, Jun
AU - Sato, Takato
AU - Takano, Mitsunori
N1 - Publisher Copyright:
© 2016 American Physical Society.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2016/7/13
Y1 - 2016/7/13
N2 - 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.
AB - 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.
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U2 - 10.1103/PhysRevE.94.012406
DO - 10.1103/PhysRevE.94.012406
M3 - Article
C2 - 27575163
AN - SCOPUS:84979249490
SN - 2470-0045
VL - 94
JO - Physical Review E
JF - Physical Review E
IS - 1
M1 - 012406
ER -