Protein side-chain dynamics observed by solution- and solid-state NMR: comparative analysis of methyl 2H relaxation data.
Rapid advances in solid-state MAS NMR made it possible to probe protein dynamics on a per-residue basis, similar to solution experiments. In this work we compare methyl 2H relaxation rates measured in the solid and liquid samples of alpha-spectrin SH3 domain. The solution data are treated using a model-free approach to separate the contributions from the overall molecular tumbling and fast internal motion. The latter part forms the basis for comparison with the solid-state data. Although the accuracy of solid-state measurements is limited by deuterium spin diffusion, the results suggest a significant similarity between methyl dynamics in the two samples. This is a potentially important observation, preparing the ground for combined analysis of the dynamics data by solid- and solution-state NMR.
Reif
Bernd
B
Forschunginstitut für Molekulare Pharmakologie, Robert-Rössle-Str. 10, 13125 Berlin, Germany.
Xue
Yi
Y
Agarwal
Vipin
V
Pavlova
Maria S
MS
Hologne
Maggy
M
Diehl
Anne
A
Ryabov
Yaroslav E
YE
Skrynnikov
Nikolai R
NR
D000818:Animals; D002645:Chickens; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D012996:Solutions; D013049:Spectrin / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics
D011994:Recombinant Proteins; D012996:Solutions; D013049:Spectrin