Swiss Science Concentrates

L. Frey, S. Hiller, R. Riek*, and S. Bibow*, J. Am. Chem. Soc. 2018, 140, 15402. ETH Zurich and University of Basel Lipid dynamics are crucial for membrane protein function and can therefore impact biological activity. The groups of Bibow and Riek have employed N-based NMR timescale-specific relaxation techniques with residue-resolution to obtain a better understanding of the effects of lipid dynamics on membrane proteins on milli-, micro-, nano-, and picosecond timescales. This study demonstrated how changes in lipid ordering by temperature or cholesterol were translated to the embedded protein. Time-scalespecific changes to the protein’s N-values were specific to lipid phases thatexhibiteddifferent transgauche isomerization rates, segmental and rotational motion, and fluidity. These results open the door to understanding the coupling of lipid membrane and membrane protein dynamics.