corner
corner

Phys. Rev. Lett. 100, 018107 (2008) [4 pages]

Hydrodynamic Description of Protein Folding

Download: PDF (657 kB) Buy this article Export: BibTeX or EndNote (RIS)

Sergei F. Chekmarev1,2,*, Andrey Yu. Palyanov1, and Martin Karplus3,4,†
1Institute of Thermophysics, SB RAS, 630090 Novosibirsk, Russia
2Department of Physics, Novosibirsk State University, 630090 Novosibirsk, Russia
3Laboratoire de Chimie Biophysique, ISIS Université Louis Pasteur, 67000 Strasbourg, France
4Department of Chemistry & Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA

Received 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−

*chekmarev@itp.nsc.ru

marci@tammy.harvard.edu