| Literature DB >> 23000032 |
Masanori Osawa1, Koh Takeuchi, Takumi Ueda, Noritaka Nishida, Ichio Shimada.
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.Mesh:
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Year: 2012 PMID: 23000032 DOI: 10.1016/j.sbi.2012.08.007
Source DB: PubMed Journal: Curr Opin Struct Biol ISSN: 0959-440X Impact factor: 6.809