Structure and activity of NO synthase inhibitors specific to the L-arginine binding site
β Scribed by S. Ya. Proskuryakov; A. G. Konoplyannikov; V. G. Skvortsov; A. A. Mandrugin; V. M. Fedoseev
- Publisher
- Springer
- Year
- 2005
- Tongue
- English
- Weight
- 380 KB
- Volume
- 70
- Category
- Article
- ISSN
- 0006-2979
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
It is known that anionic surface residues play a role in the long-range electrostatic attraction between acetylcholinesterase and cationic ligands. In our current investigation, we show that anionic residues also play an important role in the behavior of the ligand within the active site gorge of ac
The catalytic domain structure of Streptomyces sioyaensis 1,3--glucanase (278 amino acids), a member of glycosyl hydrolase family 16 (GHF16), was determined to 1.5 A resolution in space group P2 1 2 1 2 1 . The enzyme specifically hydrolyzes the glycosidic bond of the 1,3--linked glucan substrate. T