title: Protein functional dynamics in multiple timescales as studied by NMR spectroscopy.
abstract: Protein functional dynamics are defined as the atomic thermal fluctuations or the segmental motions that are essential for the function of the biomolecule. NMR is a very versatile technique that allows obtaining quantitative information from these processes at atomic resolution. This review is focused on the use of 15N spin relaxation methods to study functional dynamics although the connections with other NMR methods and biophysical techniques will be briefly mentioned. In the first part of the chapter, methodological aspects will be considered, while a set of selected cases will be described in more detail in the second part.
authors: Structural Biology Unit, CIC bioGUNE, Derio, Spain.
authors: Gabriel
authors: G
authors: Ortega
authors: Miquel
authors: M
authors: Pons
authors: Oscar
authors: O
authors: Millet
mesh_terms: D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular
keywords: Enzyme kinetics; Functional dynamics; NMR spectroscopy; Protein allosterism