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...Expand abstract
- Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing
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Characterisation of side-chain conformational preferences in a biologically active but unfolded protein.
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