Unknown

Dataset Information

0

Violation of the fluctuation-dissipation theorem in a protein system.


ABSTRACT: We report the results of molecular dynamics simulations of the protein myosin carried out with an elastic network model. Quenching the system, we observe glassy behavior of a density correlation function and a density response function that are often investigated in structure glasses and spin glasses. In the equilibrium, the fluctuation-response relation, a representative relation of the fluctuation-dissipation theorem, holds that the ratio of the density correlation function to the density response function is equal to the temperature of the environment. We show that, in the quenched system that we study, this relation can be violated. In the case that this relation does not hold, this ratio can be regarded as an effective temperature. We find that this effective temperature of myosin is higher than the temperature of the environment. We discuss the relation between this effective temperature and energy transduction that occurs after ATP hydrolysis in the myosin molecule.

SUBMITTER: Hayashi K 

PROVIDER: S-EPMC1913139 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Violation of the fluctuation-dissipation theorem in a protein system.

Hayashi Kumiko K   Takano Mitsunori M  

Biophysical journal 20070511 3


We report the results of molecular dynamics simulations of the protein myosin carried out with an elastic network model. Quenching the system, we observe glassy behavior of a density correlation function and a density response function that are often investigated in structure glasses and spin glasses. In the equilibrium, the fluctuation-response relation, a representative relation of the fluctuation-dissipation theorem, holds that the ratio of the density correlation function to the density resp  ...[more]

Similar Datasets

| S-EPMC7250396 | biostudies-literature
| S-EPMC9156749 | biostudies-literature
| S-EPMC5775451 | biostudies-literature
| S-EPMC8262459 | biostudies-literature
| S-EPMC1752236 | biostudies-literature
| S-EPMC6333177 | biostudies-literature
| S-EPMC4479990 | biostudies-other
| S-EPMC9200729 | biostudies-literature
| S-EPMC5338409 | biostudies-literature
| S-EPMC5187426 | biostudies-literature