title: NMR contributions to structural dynamics studies of intrinsically disordered proteins.
abstract: Intrinsically disordered proteins (IDPs) are characterized by substantial conformational plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to study these proteins. In contrast, NMR spectroscopy offers unique opportunities for structural and dynamic studies of IDPs. The past two decades have witnessed significant development of NMR spectroscopy that couples advances in spin physics and chemistry with a broad range of applications. This article will summarize key advances in basic physical-chemistry and NMR methodology, outline their limitations and envision future R&D directions.
authors.affiliation: Department of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria. Electronic address: robert.konrat@univie.ac.at.
authors.forename: Robert
authors.initials: R
authors.lastname: Konrat
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D015195:Drug Design; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation
chemical_list: D064267:Intrinsically Disordered Proteins
keywords: Biomolecular NMR; EPR spectroscopy; Intrinsically disordered proteins; NMR spin relaxation; Protein meta-structure; Structural biology