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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
Division:
MPLS
Department:
Chemistry
Sub department:
Inorganic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
Journal:
Journal of biomolecular NMR More from this journal
Volume:
19
Issue:
2
Pages:
153-165
Publication date:
2001-02-01
DOI:
EISSN:
1573-5001
ISSN:
0925-2738
Language:
English
Keywords:
Pubs id:
pubs:37726
UUID:
uuid:bcda082e-230b-43e2-8482-82f4bd819330
Local pid:
pubs:37726
Source identifiers:
37726
Deposit date:
2012-12-19

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