๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Predicting relative binding affinities of non-peptide HIV protease inhibitors with free energy perturbation calculations

โœ Scribed by Margaret A. McCarrick; Peter A. Kollman


Book ID
110257852
Publisher
Springer Netherlands
Year
1999
Tongue
English
Weight
240 KB
Volume
13
Category
Article
ISSN
0920-654X

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Calculation of relative binding affiniti
โœ Ravichandra Mutyala; R. N. Reddy; M. Sumakanth; P. Reddanna; M. Rami Reddy ๐Ÿ“‚ Article ๐Ÿ“… 2007 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 185 KB

## Abstract The free energy perturbation (FEP) methodology is the most accurate means of estimating relative binding affinities between inhibitors and protein variants. In this article, the importance of hydrophobic and hydrophilic residues to the binding of adenosine monophosphate (AMP) to the fru

Peptide mimetics as enzyme inhibitors: U
โœ Piotr Cieplak; Peter A. Kollman ๐Ÿ“‚ Article ๐Ÿ“… 1993 ๐Ÿ› Springer Netherlands ๐ŸŒ English โš– 935 KB

We present the application of free energy perturbation theory/molecular dynamics to predict the consequence of replacing each of the seven peptide bonds in the potent HIV protease inhibitor JG365: ACE (acetyl)-Ser-Leu-Asn-HEA (hydroxyethylamine analog of Phe-Pro)-Ile-Val-NME (N-methyl) by ethylene o

Accurate prediction of protonation state
โœ Kitiyaporn Wittayanarakul; Supot Hannongbua; Michael Feig ๐Ÿ“‚ Article ๐Ÿ“… 2008 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 531 KB

## Abstract Binding free energies were calculated for the inhibitors lopinavir, ritonavir, saquinavir, indinavir, amprenavir, and nelfinavir bound to HIVโ€1 protease. An MMPB/SAโ€type analysis was applied to conformational samples from 3 ns explicit solvent molecular dynamics simulations of the enzym