Swiss Science Concentrates

摘要

Lipid dynamics are crucial for membrane protein function and can therefore impact biological activity. The groups of Bibow and Riek have employed ~(15)N-based NMR time-scale-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-scale-specific changes to the protein's ~(15)N-values were specific to lipid phases that exhibited different trans-gauche isomerization rates, segmental and rotational motion, and fluidity. These results open the door to understanding the coupling of lipid membrane and membrane protein dynamics.