Abstract
The dynamics of proteins and biopolymers play a crucial role in their function. By using Brownian dynamics we show that polymer globules, which serve as a model system for proteins, undergo a size-dependent dynamical transition from a liquid-like state at high to a frozen state at low with a relaxation time that diverges at the transition point. Furthermore, a stretch-induced melting transition is shown to be readily controlled by external forces that exploit the polymer connectivity to modify the size of the globule. This pathway could be a general route to enhance the rate of conformational changes in naturally occurring biopolymers.
- Received 11 January 2011
DOI:https://doi.org/10.1103/PhysRevE.83.040801
©2011 American Physical Society