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Default Functional dynamics of proteins revealed by solution NMR

Functional dynamics of proteins revealed by solution NMR

October 2012
Publication year: 2012
Source:Current Opinion in Structural Biology, Volume 22, Issue 5



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.
Highlights

? Solution NMR can analyze the dynamics of proteins over a wide range of timescales. ? Recent progresses in a variety of NMR techniques are reviewed. ? Relaxation dispersion and PRE are capable of discerning ‘invisible’ low-populated states. ? NMR applications to functionally relevant protein dynamics are also introduced.





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