Conversion of the reactive sulfhydryl groups of proteins to the S-trifluoroethyl derivatives
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference18 articles.
1. Study of cooperative interactions in hemoglobin using fluorine nuclear magnetic resonance
2. A Spectroscopic Investigation of S-Trifluoroethylthiopapain. An Investigation of the Active Site of Papain
3. 19 F NMR probes for proteins; S -trifluoromethylmercuri-papain
4. Co-operative Ionisation of Aspartic-Acid-158 and Histidine-159 in Papain. Evidence from 19 F Nuclear-Magnetic-Resonance and Fluorescence Spectroscopy
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1. Soluble Methane Monooxygenase Component Interactions Monitored by 19F NMR;Biochemistry;2021-06-08
2. The effects of cleavage of the inter-chain disulphide bonds of rabbit IgG on its ability to bind C1q;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1984-05
3. Application of 19F NMR spectroscopy to a study of carbon monoxide binding to human hemoglobin modified at cys-β93 with the S-trifluoroethyl residue;Archives of Biochemistry and Biophysics;1984-04
4. Activation of the binding of C1q to immune complexes by zinc;FEBS Letters;1983-10-03
5. Evidence for histidine residues in the immunoglobulin-binding site of human C1q;Bioscience Reports;1983-02-01
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