Two molecular dynamics simulations ( 100 and 50 ps) of native porcine pancreatic elastase i.e., without bound substrate and with the active site hydrated by a dome of water (630 molecules ) have been performed. Dynamical properties of the catalytic tetrad have been examined. While relative conformat
Dynamical analysis of the conformation of the active site of porcine pancreatic elastase in native and Michaelis complex states. Molecular dynamics simulations
✍ Scribed by M. Geller; A. Ła̧czkowski; S.M. Swanson; E.F. Meyer Jr
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- English
- Weight
- 853 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0097-8485
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
A 31.5 picosecond (ps) MD calculation has been completed for the 1 : 1 enzyme-ligand complex between porcine pancreatic elastase (PPE) and acetyl-alanine-proline-alanine (APA). The 1 : 2 complex studied crystallographically a t product saturation conditions precludes the study of a 1 : 1 complex (PP
The molecular dynamics (MD) simulation of superoxide dismutase (SOD) in water is carried out for a total of 23 ps. The simulation system is a 26 A sphere centered at the active site of SOD, including 1602 atoms from SOD and 1761 water molecules. There is no gross deviation from the x-ray structure f