Editorial on molecular dynamics simulations
β Scribed by Eaton E. Lattman
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 25 KB
- Volume
- 42
- Category
- Article
- ISSN
- 0887-3585
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A molecular force field dedicated to molecular dynamics simulation of biomembranes was developed. It was parameterized on model compounds related to phospholipids and was able to reproduce at the same time structures, energies, and vibrational spectra. Cross terms in the potential energy function we
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
## Abstract The histidineβcontaining protein (HPr) plays an important role in the phosphotransferase system (PTS). The deformations induced on the protein structure at high hydrostatic pressure values (4, 50, 100, 150, and 200 MPa) were previously (H. Kalbitzer, A. GΓΆrler, H. Li, P. Dubovskii, A. H
This article considers the treatment of long-range interactions in molecular dynamics simulations. We investigate the effects of using different cutoff distances, constant versus distancedependent dielectric, and different smoothing methods. In contrast to findings of earlier studies, we find that i
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