Describing intrinsically disordered proteins at atomic resolution by NMR.

Abstract : There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from nuclear magnetic resonance spectroscopy are presented. Ensemble approaches are particularly well adapted to map the conformational energy landscape sampled by the protein at atomic resolution. Significant advances in development of calibrated approaches to the statistical representation of the conformational behaviour of IDPs are presented, as well as applications to some biologically important systems where disorder plays a crucial role.
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Current Opinion in Structural Biology, Elsevier, 2013, 23 (3), pp.426-35. 〈10.1016/j.sbi.2013.02.007〉
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Soumis le : jeudi 26 mai 2016 - 09:43:25
Dernière modification le : jeudi 11 janvier 2018 - 06:15:24

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Malene Ringkjøbing Jensen, Rob W H Ruigrok, Martin Blackledge. Describing intrinsically disordered proteins at atomic resolution by NMR.. Current Opinion in Structural Biology, Elsevier, 2013, 23 (3), pp.426-35. 〈10.1016/j.sbi.2013.02.007〉. 〈hal-01321604〉

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