Journal
PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
Volume 102, Issue -, Pages 43-60Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.pnmrs.2017.06.001
Keywords
Protein dynamics; Intrinsically disordered protein; Nuclear magnetic resonance; Spin relaxation; Segmental motion; Arrhenius relationship; Activation energy
Funding
- Agence Nationale de Recherche
- Swiss National Science Foundation Early Postdoc Mobility Fellowship [P2ELP2_148858]
- FRISBI [ANR-10-INSB-05-02]
- GRAL within the Grenoble Partnership for Structural Biology (PSB) [ANR-10-LABX-49-01]
- Swiss National Science Foundation (SNF) [P2ELP2_148858] Funding Source: Swiss National Science Foundation (SNF)
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Nuclear magnetic resonance (NMR) spectroscopy is one of the most powerful experimental approaches for investigating the conformational behaviour of intrinsically disordered proteins (IDPs). IDPs represent a significant fraction of all proteomes, and, despite their importance for understanding fundamental biological processes, the molecular basis of their activity still remains largely unknown. The functional mechanisms exploited by IDPs in their interactions with other biomolecules are defined by their intrinsic dynamic modes and associated timescales, justifying the considerable interest over recent years in the development of technologies adapted to measure and describe this behaviour. NMR spin relaxation delivers information-rich, site-specific data reporting on conformational fluctuations occurring throughout the molecule. Here we review recent progress in the use of N-15 relaxation to identify local backbone dynamics and long-range chain-like motions in unfolded proteins. (C) 2017 Elsevier B.V. All rights reserved.
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