Describing intrinsically disordered proteins at atomic resolution by NMR

• Published in: Current opinion in structural biology Vol. 23; no. 3; pp. 426 - 435
• Main Authors: Jensen, Malene Ringkjøbing, Ruigrok, Rob WH, Blackledge, Martin
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.06.2013; Elsevier
• Subjects: Biochemistry, Molecular Biology; Intrinsically Disordered Proteins; Intrinsically Disordered Proteins - chemistry; Life Sciences; Nuclear Magnetic Resonance, Biomolecular; Nuclear Magnetic Resonance, Biomolecular - methods; Protein Conformation; Protein Folding; Structural Biology
• ISSN: 0959-440X; 1879-033X
• DOI: 10.1016/j.sbi.2013.02.007

► NMR spectroscopy is a powerful tool for the study of IDPs at atomic resolution. ► NMR probes the potential energy landscape of IDPs at short-range and long-range distances. ► IDP conformational space can be mapped using NMR and ensemble descriptions. ► Flexibility of IDPs allows their NMR observation even in large molecular complexes. 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.