Periodic force induced stabilization or destabilization of the denatured state of a protein
arXiv:1205.6638 · doi:10.1063/1.3635774
Abstract
We have studied the effects of an external sinusoidal force in protein folding kinetics. The externally applied force field acts on the each amino acid residues of polypeptide chains. Our simulation results show that mean protein folding time first increases with driving frequency and then decreases passing through a maximum. With further increase of the driving frequency the mean folding time starts increasing as the noise-induced hoping event (from the denatured state to the native state) begins to experience many oscillations over the mean barrier crossing time period. Thus unlike one-dimensional barrier crossing problems, the external oscillating force field induces both \emph{stabilization or destabilization of the denatured state} of a protein. We have also studied the parametric dependence of the folding dynamics on temperature, viscosity, non-Markovian character of bath in presence of the external field.
References in corpus (14)
- Artificial Brownian motors: Controlling transport on the nanoscale
- Viscosity Dependence of the Folding Rates of Proteins
- DNA unzipped under a constant force exhibits multiple metastable intermediates
- Experimental Investigation of Resonant Activation
- Scaling of folding properties in simple models of proteins
- Probing molecular free energy landscapes by periodic loading
- Langevin dynamics with dichotomous noise; direct simulation and applications
- Noise correlation-induced splitting of Kramers' escape rate from a metastable state
- Quantum escape kinetics over a fluctuating barrier
- Folding in two-dimenensional off-lattice models of proteins
- Insight into Resonant Activation in Discrete Systems
- Interference of stochastic resonances: Splitting of Kramers' rate
- Folding of the Protein Domain hbSBD
- Resonant enhancement of the jump rate in a double-well potential