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Measuring dynamic and kinetic information in the previously inaccessible Supra-tc window of nanoseconds to microseconds by solution NMR spectroscopy.

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Ban,  D.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Sabo,  T. M.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Griesinger,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Lee,  D.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Citation

Ban, D., Sabo, T. M., Griesinger, C., & Lee, D. (2013). Measuring dynamic and kinetic information in the previously inaccessible Supra-tc window of nanoseconds to microseconds by solution NMR spectroscopy. Molecules, 18(10), 11904-11937. doi:10.3390/molecules181011904.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-9B8F-E
Abstract
Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool that has enabled experimentalists to characterize molecular dynamics and kinetics spanning a wide range of time-scales from picoseconds to days. This review focuses on addressing the previously inaccessible supra-τc window (defined as τc < supra-τc < 40 μs; in which τc is the overall tumbling time of a molecule) from the perspective of local inter-nuclear vector dynamics extracted from residual dipolar couplings (RDCs) and from the perspective of conformational exchange captured by relaxation dispersion measurements (RD). The goal of the first section is to present a detailed analysis of how to extract protein dynamics encoded in RDCs and how to relate this information to protein functionality within the previously inaccessible supra-τc window. In the second section, the current state of the art for RD is analyzed, as well as the considerable progress toward pushing the sensitivity of RD further into the supra-τc scale by up to a factor of two (motion up to 25 ms). From the data obtained with these techniques and methodology, the importance of the supra-τ c scale for protein function and molecular recognition is becoming increasingly clearer as the connection between motion on the supra-τc scale and protein functionality from the experimental side is further strengthened with results from molecular dynamics simulations.