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Toward a description of the conformations of denatured states of proteins. Comparison of a random coil model with NMR measurements

Abstract:

A strategy is proposed to describe the backbone conformations sampled in denatured states of proteins. Main chain dihedral angle distributions are extracted from the protein data base and used to predict NMR parameters such as coupling constants and NOE intensities. A simple model in which each residue samples its φ,ψ distribution noncooperatively has been found to reproduce many of the features of experimental NMR data for hen egg-white lysozyme denatured in 8 M urea at low pH. This model pr...

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Publication status:
Published

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Publisher copy:
10.1021/jp952747v

Authors


Fiebig, KM More by this author
Schwalbe, H More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Dobson, CM More by this author
Journal:
JOURNAL OF PHYSICAL CHEMISTRY
Volume:
100
Issue:
7
Pages:
2661-2666
Publication date:
1996-02-15
DOI:
EISSN:
1541-5740
ISSN:
0022-3654
URN:
uuid:ba0adf3c-1513-4556-b1cb-9b24edc677ad
Source identifiers:
45092
Local pid:
pubs:45092

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