𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Motion at the active site of [(4-fluorophenyl)sulfonyl]chymotrypsin

✍ Scribed by Ando, M. E.; Gerig, J. T.; Luk, K. F. S.


Book ID
125940339
Publisher
American Chemical Society
Year
1986
Tongue
English
Weight
892 KB
Volume
25
Category
Article
ISSN
0006-2960

No coin nor oath required. For personal study only.


πŸ“œ SIMILAR VOLUMES


Dynamics at the Active Site ofN-(4-Fluor
✍ Christopher D. Johnson; J. T. Gerig πŸ“‚ Article πŸ“… 1996 πŸ› John Wiley and Sons 🌐 English βš– 779 KB

N-(4-Fluorophenyl)-N-(2,6diflnorophenyl)carbamoyl chloride was synthesized and used to inactivate the serine protease a-chymotrypsin. The derivatized enzyme reactivates sufficiently slowly at pH 5.2 that extended fluorine NMR studies of the system are possible. Such studies show that the 4-fluorophe

Dynamics at the active site of N,N-bis(2
✍ M. Kairi; J. T. Gerig πŸ“‚ Article πŸ“… 1990 πŸ› John Wiley and Sons 🌐 English βš– 812 KB

## Abstract __N,N__‐Bis(2‐fluorophenyl)carbamoyl chloride inactivates the serine protease α‐chymotrypsin by stoichiometric carbamoylation, presumably at the active site serine‐195 residue. At sample temperatures above 25Β°C fluorine NMR spectra of this enzyme derivative reveal the presence of confor