A 13C nuclear magnetic resonance study of the interaction of ligands with arginine residues in dihydrofolate reductase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference19 articles.
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4. Selectively enriched [γ-13C]-histidine as a nuclear magnetic resonance probe of enzyme structure and function. Synthesis and incorporation into E.coli alkaline phosphatase
5. Nuclear Magnetic Resonance of Rotational Mobility of Mouse Hemoglobin Labeled with [2- 13 C]Histidine
Cited by 17 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. 13C NMR of enzymes;Progress in Nuclear Magnetic Resonance Spectroscopy;1985-01
2. Carbon 13 nuclear magnetic resonance studies of Lactobacillus casei thymidylate synthetase containing biosynthetically incorporated [guanidino-13C]arginine.;Journal of Biological Chemistry;1982-04
3. Nuclear magnetic resonance study of dihydrofolate reductase labeled with [.gamma.-13C]tryptophan;Biochemistry;1981-10-13
4. Production of an aromatic amino acid auxotroph of a trimethoprim-resistant Escherichia coli and deuteration of the aromatic amino acids in its dihydrofolate;Biochimica et Biophysica Acta (BBA) - General Subjects;1981-01
5. Soybean trypsin inhibitor (Kunitz) and its complex with trypsin. Carbon-13 nuclear magnetic resonance studies of the reactive site arginine;Biochemistry;1980-12-09
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