Abstract
Establishing correlations among distant (>3 Å) spins remains an outstanding problem for both spectral assignment and elucidation of interhelical contacts in solid-state NMR of oriented membrane proteins. Here we present a pulse sequence which incorporates the previously established mismatched Hartmann–Hahn mixing of dilute spins via the proton bath together with high-resolution local field spectroscopy. In addition to providing structural information, the use of dipolar couplings in the indirect dimension helps eliminate the spectral crowdedness compared to the standard homonuclear correlation techniques. The proposed pulse sequence may find its use in assigning protein spectra in uniaxially oriented membrane environments.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
