Enzyme-inhibitor interactions studied via fluorine magnetic resonance
- 1 March 1970
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 137 (1) , 291-293
- https://doi.org/10.1016/0003-9861(70)90438-8
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
- X‐Ray Analysis, Structure and Function of EnzymesEuropean Journal of Biochemistry, 1969
- Nonpolar contributions to the rate of nucleophilic displacements of p-nitrophenyl esters in micellesJournal of the American Chemical Society, 1968
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1968
- Enzyme-inhibitor interactions studied via fluorine nuclear magnetic resonance. I. The interaction of α-chymotrypsin with DL-N-trifluoroacetylphenylalanineBiochemical and Biophysical Research Communications, 1968
- Investigation of micelle structure by fluorine magnetic resonance. II. Effects of temperature changes, added electrolyte, and counterion sizeThe Journal of Physical Chemistry, 1968
- Catalysis of Ester Hydrolysis by Mixed Micelles ContainingN-α-Myristoyl-L-HistidineScience, 1967
- Study of the Polarity of the Active Site of Chymotrypsin*Biochemistry, 1966
- Spectrophotometric Investigations of the Mechanism of α-Chymotrypsin-catalyzed Hydrolyses. Detection of the Acyl-enzyme Intermediate1-3Journal of the American Chemical Society, 1962