TY - JOUR
T1 - Functional dynamics of proteins revealed by solution NMR
AU - Osawa, Masanori
AU - Takeuchi, Koh
AU - Ueda, Takumi
AU - Nishida, Noritaka
AU - Shimada, Ichio
N1 - Funding Information:
This work was supported in part by grants from the Japan New Energy and Industrial Technology Development Organization (NEDO) and the Ministry of Economy, Trade, and Industry (METI) (to I.S.), a Grant-in-Aid for Scientific Research on Priority Areas from the Japanese Ministry of Education, Culture, Sports, Science, and Technology (to M.O., K.T., T.U., and I.S.), and a grant from Takeda Science Foundation (to M.O.).
PY - 2012/10
Y1 - 2012/10
N2 - 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.
AB - 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.
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U2 - 10.1016/j.sbi.2012.08.007
DO - 10.1016/j.sbi.2012.08.007
M3 - Review article
C2 - 23000032
AN - SCOPUS:84867745578
SN - 0959-440X
VL - 22
SP - 660
EP - 669
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 5
ER -