Effective potentials for Folding Proteins

Details Effective potentials for Folding Proteins Effective potentials for Folding Proteins

2006-01-24

arxiv.org/abs/cond-mat/0601533v2

Phys. Rev. Lett. 96, 078103 (2006)

Physics

Condensed Matter

Statistical Mechanics

4 pages, 4 figures, to appear in Physical Review Letters

Scientific paper

10.1103/PhysRevLett.96.078103

A coarse-grained off-lattice model that is not biased in any way to the native state is proposed to fold proteins. To predict the native structure in a reasonable time, the model has included the essential effects of water in an effective potential. Two new ingredients, the dipole-dipole interaction and the local hydrophobic interaction, are introduced and are shown to be as crucial as the hydrogen bonding. The model allows successful folding of the wild-type sequence of protein G and may have provided important hints to the study of protein folding.

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