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Structural and dynamical characterization of a biologically active unfolded fibronectin-binding protein from Staphylococcus aureus.

Abstract:

A 130-residue fragment (D1-D4) taken from a fibronectin-binding protein of Staphylococcus aureus, which contains four fibronectin-binding repeats and is unfolded but biologically active at neutral pH, has been studied extensively by NMR spectroscopy. Using heteronuclear multidimensional techniques, the conformational properties of D1-D4 have been defined at both a global and a local level. Diffusion studies give an average effective radius of 26.2 +/- 0.1 A, approximately 75% larger than that...

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Publication status:
Published

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Publisher copy:
10.1021/bi9814080

Authors


Penkett, CJ More by this author
Redfield, C More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Physics, Atomic and Laser Physics
Hubbard, J More by this author
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Journal:
Biochemistry
Volume:
37
Issue:
48
Pages:
17054-17067
Publication date:
1998-12-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:3ba8b860-aaac-4c1a-a387-7ba24b4face3
Source identifiers:
10904
Local pid:
pubs:10904

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