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Office: JE 376
Phone: (614) 688-0427
Email: psrinivasan@mbi.osu.edu
Mentors: Avner Friedman (Mathematics), Philip Grandinetti
(Chemistry)
Research Area
Membrane proteins are proteins that reside in the membranes of cells. They
form an important class of proteins because they are central to a variety
of cellular processes. As the functionality of proteins is closely related
to its 3-dimensional structure, there is a huge amount of interest in
obtaining structures of membrane proteins. Due to the gel-like nature of
the membrane environment, it is hard to crystallize membrane proteins in
their native environment in order to perform X-ray crystallography on
them. Nuclear magnetic resonance (NMR) is becoming an increasingly popular
tool to obtain high-resolution structures of membrane proteins by
providing distance and orientation information among the various spins
(atoms) residing in the backbone of a protein. Due to the variety of spin
interactions present in solid biological samples, it is important to
suppress undesired interactions, while keeping the ones of interest. In NMR,
this is achieved through a technique called pulse sequences. I have
previously worked in the quantum mechanical analysis of pulse sequences. I
am interested in designing new pulse sequences and/or modifying existing
ones that improve the resolution and sensitivity of solid-state NMR
experiments of biological samples.
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