Probing the Abilities of Synthetically Useful Serine Proteases To Discriminate between the Configurations of Remote Stereocenters Using Chiral Aldehyde Inhibitors
- 1 January 1996
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 118 (3) , 502-508
- https://doi.org/10.1021/ja952835t
Abstract
No abstract availableThis publication has 46 references indexed in Scilit:
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Crystal and molecular structure of the bovine α-chymotrypsin-eglin c complex at 2.0 Å resolutionJournal of Molecular Biology, 1992
- Probing the specificity of the S1 binding site of subtilisin Carlsberg with boronic acidsBiochemical and Biophysical Research Communications, 1991
- Enzymatic synthesis of amides with two chiral centresJournal of the Chemical Society, Chemical Communications, 1990
- Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineeringJournal of Molecular Biology, 1987
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- Peptide aldehydes inhibiting chymotrypsinBiochemical and Biophysical Research Communications, 1972
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1972
- Studies in Stereochemistry. VI. The Mechanisms of the E1 and Hydrogen Migration Reactions in the 3-Phenyl-2-butanol SystemJournal of the American Chemical Society, 1952
- The Ultraviolet Absorption Spectra of α-Phenylcarbonyl Compounds1Journal of the American Chemical Society, 1950