Analysis of the binding of 1,3-diacetylchloramphenicol to chloramphenicol acetyltransferase by isotope-edited proton NMR and site-directed mutagenesis
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00150a010
Reference20 articles.
1. Identification of the C2-1H histidine NMR resonances in chloramphenicol acetyltransferase by a13C-1H heteronuclear multiple quantum coherence method
2. Intrinsic fluorescence of chloramphenicol acetyltransferase: responses to ligand binding and assignment of the contributions of tryptophan residues by site-directed mutagenesis
3. Substrate binding to chloramphenicol acetyltransferase: evidence for negative cooperativity from equilibrium and kinetic constants for binary and ternary complexes
4. Isotope-edited proton NMR study on the structure of a pepsin/inhibitor complex
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