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Challenges measuring distances between metal centers in proteins using pulsed electron paramagnetic resonance

Electron paramagnetic resonance (EPR) spectroscopy provides electronic and structural information on paramagnets, which often serve structural and/or functional roles in biomacromolecules. Double electron-electron resonance (DEER) spectroscopy is a pulsed EPR technique used to measure distances between two or more paramagnetic centers. Such sites can be intrinsic or be engineered into a biological system of interest. Measurement of the inter-paramagnet distances provides structural information that often cannot be obtained using other structural biology methods. Recent advances in DEER have utilized paramagnetic metal ions to achieve greater resolution and distance range. When metal-binding sites are engineered into a biomacromolecule, special tags often are required, which limits metal ion placement and complicates data interpretation. In my talk, I will present a brief history of EPR spectroscopy of metal ions in proteins, including the requirements and benefits of metal centers for DEER. My current research explores the feasibility of performing DEER on metal ions using intrinsic binding sites within proteins, eliminating the necessity of added tags.

For further information please contact Veronika Szalai, 301-975-3792, veronika.szalai [at] nist.gov

Sponsors

Veronika Szalai, 301-975-3792, veronika.szalai [at] nist.gov

Virginia Meyer

Protein NMR Section, Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, NIH

Created October 14, 2015, Updated May 13, 2016