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Chemistry receives two NIH instrumentation grants for solid state NMR and pulsed EPR

bryant22cafiso2Profs. Robert Bryant and David Cafiso secured two NIH instrumentation grants to increase our magnetic resonance research capacity.

Prof. Bryant (along with Profs. Columbus, Cafiso, and Tamm) received $450,960 for a new four-channel NMR console to be used in conjunction with an existing 11.7 T narrow bore super conducting magnet to create a new spectrometer capable of state-of-the-art NMR experiments on solid samples. This instrument will facilitate the study of proton-spin dynamics in protein systems that are critical to understanding the spin-physics of contrast development in MRI as well as the internal energy landscape in proteins as affected by local water- protein interactions.  The instrument will be applied to examine:

  • membrane docking of tandem C2 domains from synaptotagamin and to examine the problem of lipid de-mixing at the lipid-protein interface
  • the dynamics and assembly of the Opa proteins in bilayers and provide structural and dynamical characterization of the key recognition sites for engulfment of bacteria by the host cells
  • membrane-protein interactions and lipid order in membrane fusion problems including SNARE-mediated membrane fusion events that are important in understanding the infection process.

Prof. Cafiso (along with Profs. Bryant, Columbus, Tamm, and Nakamoto) received $500,000 to upgrade an existing Bruker Elexsys 500 continuous wave EPR spectrometer to add pulse capability. The upgraded instrument will be a highly versatile EPR instrument that will _dsc7742be capable of a broad range of pulse experiments with ns time resolution, but will retain the ability to run in CW mode. This instrument is also capable of saturation recovery as well as ELDOR experiments. The instrument will be used to obtain information on the structure and dynamics of membrane proteins, and large protein complexes. This information will be used to determine the structures and structural changes in proteins that facilitate transport across biological membranes, the structures and mechanisms of proteins that facilitate membrane attachment in cell-signaling systems, and the mechanisms of protein- mediated membrane fusion.