Enzyme-inhibitor interactions studied via fluorine magnetic resonance
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference11 articles.
1. Enzyme-inhibitor interactions studied via fluorine nuclear magnetic resonance. I. The interaction of α-chymotrypsin with DL-N-trifluoroacetylphenylalanine
2. Spectrophotometric Investigations of the Mechanism of α-Chymotrypsin-catalyzed Hydrolyses. Detection of the Acyl-enzyme Intermediate1-3
3. Study of the Polarity of the Active Site of Chymotrypsin*
4. X-Ray Analysis, Structure and Function of Enzymes
5. Structure of crystalline α-chymotrypsin
Cited by 11 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Fluorine Magnetic Resonance in Biochemistry;Biological Magnetic Resonance;1978
2. [13] Fluorine nuclear magnetic resonance studies of proteins;Methods in Enzymology;1978
3. Fluorine nuclear magnetic resonance studies of trifluoroacetylinsulin derivatives effects of salts and denaturants;Biochimica et Biophysica Acta (BBA) - Protein Structure;1976-08
4. Nonideality of mixing of micelles of fluorocarbon and hydrocarbon surfactants and evidence of partial miscibility from differential conductance data;The Journal of Physical Chemistry;1976-06
5. Fluorine nuclear magnetic resonance studies of trifluoroacetyl-insulin derivatives. Effect of pH on conformation and aggregation;Biochemistry;1974-07
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