- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1006/jmbi.1999.2722
-
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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
- Language:
- English
- Keywords:
- Copyright date:
- 1999
Journal article
Side-chain conformations in an unfolded protein: chi1 distributions in denatured hen lysozyme determined by heteronuclear 13C, 15N NMR spectroscopy.
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