Protein side-chain dynamics observed by solution- and solid-state NMR: comparative analysis of methyl 2H relaxation data |
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Authors: | Reif Bernd Xue Yi Agarwal Vipin Pavlova Maria S Hologne Maggy Diehl Anne Ryabov Yaroslav E Skrynnikov Nikolai R |
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Affiliation: | Forschunginstitut für Molekulare Pharmakologie, Robert-R?ssle-Str. 10, 13125 Berlin, Germany. |
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Abstract: | 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. |
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