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Characterisation of side-chain conformational preferences in a biologically active but unfolded protein.

Abstract:

A combination of experimental NMR 3J alpha beta coupling constant measurements and theoretical predictions from a statistical model for a random coil have been used to characterise the conformations of amino acid side-chains in an unfolded fibronectin binding protein. The statistical model uses the distribution of torsion angles in a data base of native folded protein structures to provide a description of the torsion angle populations of each residue in a random coil. For all but three of th...

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
Journal:
Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing
Pages:
542-553
Publication date:
1999-01-01
ISSN:
2335-6936
URN:
uuid:99bf3801-948f-42b1-be17-255583d5957a
Source identifiers:
31511
Local pid:
pubs:31511

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