Molecular Dynamics Simulation of Peptide Folding
β Scribed by Xavier Daura
- Publisher
- John Wiley and Sons
- Year
- 2007
- Weight
- 11 KB
- Volume
- 38
- Category
- Article
- ISSN
- 0931-7597
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π SIMILAR VOLUMES
Molecular dynamics simulations of β€-hairpin folding have been carried out with a solvent-referenced potential at 274 K. The model peptide V 4 D PGV 4 formed stable β€-hairpin conformations and the β€-hairpin ratio calculated by the DSSP algorithm was about 56% in the 50-ns simulation. Folding into β€-h
We have performed 128 folding and 45 unfolding molecular dynamics runs of chymotrypsin inhibitor 2 (CI2) with an implicit solvation model for a total simulation time of 0.4 microseconds. Folding requires that the three-dimensional structure of the native state is known. It was simulated at 300 K by