Nuclear magnetic resonance study of interaction of ligands with Streptococcus faecium dihydrofolate reductase labeled with [.gamma.-13C]tryptophan
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00261a040
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1. Solution structure of folic acid;Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy;2004-06
2. Role of the conserved active site residue tryptophan-24 of human dihydrofolate reductase as revealed by mutagenesis;Biochemistry;1991-02-05
3. Spin-label-induced selective carbon-13 nuclear relaxation: structures of the .gamma.-cyclodextrin-tempone and .alpha.-cyclodextrin-di-tert-butyl nitroxide inclusion complexes in solution;Macromolecules;1989-10
4. Nuclear magnetic resonance study of the state of protonation of inhibitors bound to mutant dihydrofolate reductase lacking the active-site carboxyl;Biochemistry;1986-11-04
5. NMR Studies of Amino Acids, Peptides, and Proteins: A Brief Review, 1980-1982;Annual Reports on NMR Spectroscopy;1985
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