Measuring Dynamic and Kinetic Information in the Previously Inaccessible Supra-τc Window of Nanoseconds to Microseconds by Solution NMR Spectroscopy

Molecules

David Ban¹  T. Michael Sabo¹  Christian Griesinger² 

[1] id="af1-molecules-18-11904">Department for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, German

关键词: supra-τ_c;    RDC;    relaxation dispersion;    R_1ρ;    CPMG;    protein dynamics;    NMR spectroscopy;   

DOI  :  10.3390/molecules181011904

来源: mdpi

【 摘 要 】

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-τ_c window (defined as τ_c < supra-τ_c < 40 μs; in which τ_c 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-τ_c 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-τ_c scale by up to a factor of two (motion up to 25 μs). 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-τ_c scale and protein functionality from the experimental side is further strengthened with results from molecular dynamics simulations.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland.