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Side-chain conformations in an unfolded protein: chi1 distributions in denatured hen lysozyme determined by heteronuclear 13C, 15N NMR spectroscopy.

Abstract:

Using a 13C and 15N-labelled sample, multi-dimensional heteronuclear NMR techniques have been carried out to characterise hen lysozyme denatured in 8 M urea at pH 2.0. The measurement of 3J(C',Cgamma) and 3J(N,Cgamma) coupling constants has enabled side-chain chi1 torsion angle populations to be probed in the denatured polypeptide chain. Analysis of the coupling constant data has allowed the relative populations of the three staggered rotamers about chi1 to be defined for 51 residues. The ami...

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Publication status:
Published

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Publisher copy:
10.1006/jmbi.1999.2722

Authors


Spencer, A More by this author
Dobson, CM More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
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Journal:
Journal of molecular biology
Volume:
288
Issue:
4
Pages:
705-723
Publication date:
1999-05-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:55412d43-2366-4abf-8b80-a33feda92f2e
Source identifiers:
36995
Local pid:
pubs:36995

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