期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 23, 期 3, 页码 426-435出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2013.02.007
关键词
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资金
- French Agence Nationale de la Recherche through the ANR SIMI7 ComplexDynamics
- French Agence Nationale de la Recherche through ANR MALZ TAUSTRUCT
- French Agence Nationale de la Recherche through JCJC ProteinDisorder
- Finovi foundation of Lyon
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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