On the mechanism of proton transfer in the catalysis by serine proteases
✍ Scribed by L. Pogár
- Publisher
- Elsevier Science
- Year
- 1971
- Tongue
- English
- Weight
- 268 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0022-5193
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Conservation of clusters of buried water molecules is a structural motif present throughout the serine protease family. Frequently, these clusters are shaped as water channels forming extensive hydrogen-bonding networks linked to the protein backbone. The most conspicuous example is the water channe
Quantum mechanical ab initio (RHF/6-31؉G\*//RHF/3-21G) calculations were used to simulate the formation of the tetrahedral complex intermediate (TC) in serine protease active site by substrates and transition-state analog inhibitors. The enzyme active site was simulated by an assembly of the amino a
## Abstract The role of water in the proton transfer mechanism between the carboxylic and the amino group in tryptophan was studied through the direct, intramolecular reaction in presence of a continuum and the single water molecule mediated, intermolecular reaction in vacuum and in presence of a c