Phys. Rev. Lett. 100, 018107 (2008) [4 pages]Hydrodynamic Description of Protein FoldingReceived 22 June 2007; published 11 January 2008 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 two-state folding kinetics. The flows from the unfolded to the native state are concentrated 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 associated with local minima, 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 standard analyses. © 2008 The American Physical Society URL:
http://link.aps.org/doi/10.1103/PhysRevLett.100.018107
DOI:
10.1103/PhysRevLett.100.018107
PACS:
87.14.E−, 47.85.Dh, 87.15.Cc, 87.15.H−
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