Structural biology by NMR: structure, dynamics, and interactions.

Phineus R L Markwick (1) , Thérèse Malliavin (1) , Michael Nilges (1)

1 Bioinformatique Structurale

The function of bio-macromolecules is determined by both their 3D structure and conformational dynamics. These molecules are inherently flexible systems displaying a broad range of dynamics on time-scales from picoseconds to seconds. Nuclear Magnetic Resonance (NMR) spectroscopy has emerged as the method of choice for studying both protein structure and dynamics in solution. Typically, NMR experiments are sensitive both to structural features and to dynamics, and hence the measured data contain information on both. Despite major progress in both experimental approaches and computational methods, obtaining a consistent view of structure and dynamics from experimental NMR data remains a challenge. Molecular dynamics simulations have emerged as an indispensable tool in the analysis of NMR data.

Mots clés: Protein structure; Protein structure determination; Nuclear magnetic resonance; Biophysical simulations; NMR relaxation; Biochemical simulations; Molecular dynamics; NMR spectroscopy

Domaines: Bio-Informatique, Biologie Systémique [q-bio.QM]

Phineus R L Markwick, Thérèse Malliavin, Michael Nilges. Structural biology by NMR: structure, dynamics, and interactions.. PLoS Computational Biology, 2008, 4 (9), pp.e1000168. ⟨10.1371/journal.pcbi.1000168⟩. ⟨pasteur-01570032⟩