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1H-NMR characterization of L-tryptophan binding to TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis.

Abstract:

A 1H-NMR study of the binding of L-tryptophan to the trp RNA-binding attenuation protein of Bacillus subtilis (TRAP), an ondecamer (91.6 kDa), has been implemented. The assignment of the aromatic indole ring proton resonances of the bound tryptophan ligand has been successfully carried out by two-dimensional chemical exchange experiments. The observation of only a single set of chemical shifts of the bound ligand demonstrates that the tryptophan binding site is identical in all the 11 subunit...

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Publication status:
Published

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Journal:
The Biochemical journal
Volume:
315 ( Pt 3)
Issue:
3
Pages:
895-900
Publication date:
1996-05-05
EISSN:
1470-8728
ISSN:
0264-6021
URN:
uuid:17262da6-594d-4eb0-ad7b-4759a189814b
Source identifiers:
400291
Local pid:
pubs:400291

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