Hydrodynamic description of protein folding
Publication information:
Chekmarev S, Palyanov A, Karplus M. Hydrodynamic description of protein folding. Phys. Rev. Lett. 2008;100(1):018107/1–018107/4.
Abstract
A hydrodynamic description of protein folding is proposed and illustrated with a lattice protein model, which has a free energy surface (FES) typical of proteins with 2-state folding kinetics. The flows from the unfolded to the native state are concd. in a limited region of the FES. The rest is occupied by a flow "vortex", which does not lead to the native state. In contrast, with intermediates that are assocd. with local min., the vortex is not visible on the FES. The hydrodynamic interpretation thus provides new insights into the mechanism of protein folding and can be a useful complement to std. analyses.