Skip to Main content Skip to Navigation
Journal articles

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.
Complete list of metadata

https://hal.univ-grenoble-alpes.fr/hal-01321604
Contributor : Frank Thomas Connect in order to contact the contributor
Submitted on : Thursday, May 26, 2016 - 9:43:25 AM
Last modification on : Saturday, June 25, 2022 - 8:27:46 PM

Identifiers

Collections

Citation

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⟩

Share

Metrics

Record views

51