Abstract
Pulsed Electron Paramagnetic Resonance (EPR) spectroscopic techniques such as Double Electron-Electron Resonance (DEER) can provide pertinent structural information on a wide variety of biological systems that have been spin-labeled. This powerful technique can be used to measure distances between 2 spin labels out to about 70 A. However, the application of DEER spectroscopy to study membrane proteins can be difficult due to short phase memory times (Tm) and weak DEER modulation in more biologically relevant proteoliposomes when compared to water soluble proteins or membrane proteins in detergent micelles. The combination of these factors often leads to broad distance distributions, poor signal to noise, and limitations in the determination of longer distances. The short phase memory times are typically due to uneven distributions of spin-labeled protein within the lipid bilayer, which creates local inhomogeneous pockets of high spin concentrations. Approaches to overcome these limitations and improve the quality of DEER measurements for membrane proteins will be discussed: lipodisq nanoparticles, bi-functional spin labels (BSL), and Q-band pulsed EPR spectroscopy.
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.
