Direct prediction of NMR residual dipolar couplings from the primary sequence of unfolded proteins.

Abstract : Conformational analysis: an approach to the prediction of RDCs from disordered protein chains, integrating the effect of nearest neighbors and the alignment characteristics of the statistical coil, is reported. NMR residual dipolar couplings (RDC) are sensitive probes of conformational sampling in unfolded proteins.
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Angewandte Chemie (English Edition), John Wiley & Sons, 2013, 52 (2), pp.687-90. 〈10.1002/anie.201206585〉
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http://hal.univ-grenoble-alpes.fr/hal-01321602
Contributeur : Frank Thomas <>
Soumis le : jeudi 26 mai 2016 - 09:41:14
Dernière modification le : jeudi 11 janvier 2018 - 06:15:24

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Jie-Rong Huang, Valéry Ozenne, Malene Ringkjøbing Jensen, Martin Blackledge. Direct prediction of NMR residual dipolar couplings from the primary sequence of unfolded proteins.. Angewandte Chemie (English Edition), John Wiley & Sons, 2013, 52 (2), pp.687-90. 〈10.1002/anie.201206585〉. 〈hal-01321602〉

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