title: Functional dynamics of proteins revealed by solution NMR.
abstract: Solution NMR spectroscopy can analyze the dynamics of proteins on a wide range of timescales, from picoseconds to even days, in a site-specific manner, and thus its results are complementary to the detailed but largely static structural information obtained by X-ray crystallography. We review recent progresses in a variety of NMR techniques, including relaxation dispersion and paramagnetic relaxation enhancement (PRE), that permit the observation of the low-populated states, which had been 'invisible' with other techniques. In addition, we review how NMR spectroscopy can be used to elucidate functionally relevant protein dynamics.
authors.affiliation: Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
authors.forename: Masanori
authors.initials: M
authors.lastname: Osawa
authors.forename: Koh
authors.initials: K
authors.lastname: Takeuchi
authors.forename: Takumi
authors.initials: T
authors.lastname: Ueda
authors.forename: Noritaka
authors.initials: N
authors.lastname: Nishida
authors.forename: Ichio
authors.initials: I
authors.lastname: Shimada
mesh_terms: D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D012996:Solutions
chemical_list: D011506:Proteins; D012996:Solutions