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NMR processing:
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Ab initio:
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Fragment-based:
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Refinement:
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Structure from chemical shifts:
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Disordered proteins:
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Format conversion & validation:
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From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
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Isotope labeling:
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Default Identification of the C2-1H histidine NMR resonances in chloramphenicol acetyltransfe

Identification of the C2-1H histidine NMR resonances in chloramphenicol acetyltransferase by a 13C-1H heteronuclear multiple quantum coherence method.

Related Articles Identification of the C2-1H histidine NMR resonances in chloramphenicol acetyltransferase by a 13C-1H heteronuclear multiple quantum coherence method.

FEBS Lett. 1991 Mar 11;280(1):125-8

Authors: Derrick JP, Lian LY, Roberts GC, Shaw WV

Chloramphenicol acetyltransferase (CAT) was used to assess the feasibility of study of specific proton resonances in an enzyme of overall molecular mass 75,000, [ring 2-13C]Histidine was selectively incorporated into the type III chloramphenicol acetyltransferase (CATIII) using a histidine auxotroph of E. coli. Heteronuclear multiple and single quantum experiments were used to select the C2 protons in the histidyl imidazole ring. One- and two-dimensional spectra revealed six signals out of a total of seven histidine residues in CATIII. pH titration, chemical modification and ligand binding were used to demonstrate that the signal from H195, the histidine at the active site, is not among those observed. Nevertheless, this work demonstrates that selective isotopic enrichment and multiple quantum coherence techniques can be used to distinguish proton resonances in a protein of high molecular mass.

PMID: 2053974 [PubMed - indexed for MEDLINE]



Source: PubMed
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