Visualization of energetics and conformations from molecular computer simulations
โ Scribed by Paul K Weiner; Steven L Gallion; Eric Westhof; Ronald M Levy
- Publisher
- Elsevier Science
- Year
- 1986
- Tongue
- English
- Weight
- 690 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0263-7855
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๐ SIMILAR VOLUMES
## Abstract For Abstract see ChemInform Abstract in Full Text.
A significant fraction of the socalled ''random coil'' residues in globular proteins exists in the left-handed poly(Pro)II conformation. In order to compare the behavior of this secondary structure with that of the other regular secondary structures, molecular dynamics simulations, with the GROMOS s
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