Fast in silico protein folding by introduction of alternating hydrogen bond potentials.
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ABSTRACT:
SUBMITTER: Wolf MG
PROVIDER: S-EPMC2367207 | biostudies-literature | 2008 May
REPOSITORIES: biostudies-literature
Publications
Fast in silico protein folding by introduction of alternating hydrogen bond potentials.
Biophysical journal 20080501 10
We accelerate protein folding in all-atom molecular dynamics simulations by introducing alternating hydrogen bond potentials as a supplement to the force field. The alternating hydrogen bond potentials result in accelerated hydrogen bond reordering, which leads to rapid formation of secondary structure elements. The method does not require knowledge of the native state but generates the potentials based on the development of the tertiary structure in the simulation. In protein folding, the forma ...[more]
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