Hydrogen bonding in molecular recognition by HIV-1 protease
✍ Scribed by O. Aruksankunwong; S. Hannongbua; Peter Wolschann
- Publisher
- Elsevier Science
- Year
- 2006
- Tongue
- English
- Weight
- 249 KB
- Volume
- 790
- Category
- Article
- ISSN
- 0022-2860
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Benzenesulfonamides represent a hydrogen donor‐acceptor moiety that is changed to a bisacceptor by deprotonation. The dimerization constant of __N__‐tosyl‐__n__‐butylamine (7) and __N__‐tosyl‐L‐alanine (9‐H) in CDCl~3~ and the binding constant of the tetrabutylammonium salt 7·NBu~4~ to
DAAD hydrogen bond donor (D) and acceptor (A) arrays 1 were synthesized and the recognition of the complementary ADDA substrates 2 and heterodimer formation by four hydrogen bonds was measured by tH NMR titrations. The binding energy ofa sterically not crowded dimer is in accordance with the value c
## Abstract Virologic failure during treatment with raltegravir, the first effective drug targeting HIV integrase, is associated with two exclusive pathways involving either Q148H/R/K, G140S/A or N155H mutations. We carried out a detailed analysis of the molecular and structural effects of these mu
## Background: The accurate prediction of enzyme-substrate interaction energies is one of the major challenges in computational biology. this study describes the improvement of protein-ligand binding energy prediction by incorporating protein flexibility through the use of molecular dynamics (md) s
## Abstract A novel mechanism of inhibiting HIV‐1 protease (HIVp) is presented. Using computational solvent mapping to identify complementary interactions and the Multiple Protein Structure method to incorporate protein flexibility, we generated a receptor‐based pharmacophore model of the flexible