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NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein.

Abstract:

A 130-residue fragment of the Staphylococcus aureus fibronectin-binding protein has been found to exist in a highly unfolded conformation at neutral pH. Measurement of experimental NMR 3JHNalpha coupling constants provides evidence for individual residues having distinct main-chain conformational preferences that are dependent both on the amino acid concerned and on neighbouring residues in the sequence. Analysis shows that these variations in the populations of individual residues can be exp...

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Publication status:
Published

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Publisher copy:
10.1006/jmbi.1997.1369

Authors


Penkett, CJ More by this author
Redfield, C More by this author
Hubbard, J More by this author
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Journal:
Journal of molecular biology
Volume:
274
Issue:
2
Pages:
152-159
Publication date:
1997-11-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:14e25875-d8a4-4cc8-83ea-352c3b4db4da
Source identifiers:
36127
Local pid:
pubs:36127

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