Solid-state nuclear magnetic resonance (SSNMR) is a powerful tool for analyzing the structure of membrane proteins at the atomic level. Different motional regimes of the protein can be targeted with pulse sequences that take advantage of dipolar interactions and J-coupling amongst nuclei. Three mobility extremes will be considered. Cross polarization (CP) can be combined with dipolar-assisted rotational resonance (DARR) to analyze rigid alpha-helices. Oppositely, insensitive nuclear enhancement of polarization transfer (INEPT) combined with total throughbond correlation spectroscopy (TOBSY) targets flexible inter-helical loops. Lastly, the intermediate mobility regime is targeted using CP with TOBSY. The CPDARR, INEPTTOBSY, and CPTOBSY spectra for the integral membrane protein Anabaena sensory rhodopsin will be showcased, and new structural insights will be described.
Coffee and donuts will be provided. Make sure to follow the Graduate Seminar Series on Facebook.