Free Energy Component Analysis for Drug Design: A Case Study of HIV-1 Protease−Inhibitor Binding
✍ Scribed by Kalra, Parul; Reddy, T. Vasisht; Jayaram, B.
- Book ID
- 118064533
- Publisher
- American Chemical Society
- Year
- 2001
- Tongue
- English
- Weight
- 587 KB
- Volume
- 44
- Category
- Article
- ISSN
- 0022-2623
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract We have developed a simple approach for the evaluation of the free energies of inhibitor binding to the protease of the human immunodeficiency virus (HIV‐1 PR). Our algorithm is based on the observation that most groups that line the binding pockets of this enzyme are hydrophobic in nat
## Abstract Binding free energies were calculated for the inhibitors lopinavir, ritonavir, saquinavir, indinavir, amprenavir, and nelfinavir bound to HIV‐1 protease. An MMPB/SA‐type analysis was applied to conformational samples from 3 ns explicit solvent molecular dynamics simulations of the enzym