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Chemical shifts in denatured proteins: resonance assignments for denatured ubiquitin and comparisons with other denatured proteins.

Abstract:

Chemical shift assignment is reported for the protein ubiquitin denatured in 8M urea at pH 2. The variations in 15N chemical shifts of three different proteins (ubiquitin, disulfide reduced, carboxymethylated lysozyme, all-Ala-alpha-lactalbumin), all without disulfides and denatured in 8M urea at pH 2 are compared to 'random coil shifts' of small model peptides (Braun et al., 1994) and to the averaged native chemical shifts taken from the BMRB database. Both parameterizations show a remarkabl...

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Publication status:
Published

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Publisher copy:
10.1023/a:1008307323283

Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Schwalbe, H More by this author
Journal:
Journal of biomolecular NMR
Volume:
19
Issue:
2
Pages:
153-165
Publication date:
2001-02-05
DOI:
EISSN:
1573-5001
ISSN:
0925-2738
URN:
uuid:bcda082e-230b-43e2-8482-82f4bd819330
Source identifiers:
37726
Local pid:
pubs:37726

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