Effect of methylation of the histidine residue in the active site of α-chymotrypsin on the conformational stability of the enzyme
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(72)80316-8/fullpdf
Reference8 articles.
1. Structure of crystalline α-chymotrypsin
2. Structure of crystalline α-chymotrypsin
3. Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin
4. Methylation of histidine-57 in α-chymotrypsin by methyl ρ-nitrobenzenesulfonate. New approach to enzyme modification
5. Reversible filtration apparatus for concentrating protein solutions by the sephadex method
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1. CIRCULAR DICHROISM STUDIES ON NATIVE AND PHENYLMETHANESULFONYL-MESENTERICOPEPTIDASE;International Journal of Peptide and Protein Research;2009-01-12
2. Fluorine NMR of proteins;Progress in Nuclear Magnetic Resonance Spectroscopy;1994-01
3. Dynamics at the active site of N2-acetyl-N1-(4-fluorobenzyl)carbazoyl-.alpha.-chymotrypsin;Journal of the American Chemical Society;1984-12
4. Dynamics at the active site of bis(4-fluorophenyl)carbamoyl-.alpha.-chymotrypsin;Journal of the American Chemical Society;1983-07
5. Dynamics of ligand binding to .alpha.-chymotrypsin and to N-methyl-.alpha.-chymotrypsin;Biochemistry;1982-09-14
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