The research in the Lorigan laboratory is focused upon the utilization of magnetic resonance spectroscopy to investigate the structural and dynamic properties of membrane-bound proteins and peptides and their interactions within the lipid bilayer. We are specifically interested in developing and applying state-of-the-art nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopic techniques to study membrane proteins inserted into aligned phospholipid bilayers.

Membrane proteins (which make up approximately one-third of the total number of proteins) are responsible for many important properties and functions of biological systems: they transport ions and molecules across the membrane, they act as receptors, and they have roles in the assembly, fusion, and structure of cells and viruses. Despite the abundance and clear importance of these membrane proteins and peptides, only a minute amount of information regarding these systems exists.

High-resolution multi-nuclear solid-state NMR spectroscopy is a powerful technique that can yield pertinent structural, orientational, and dynamic information about membrane protein systems when they are aligned with the direction of the static magnetic field.  State-of the-art EPR spectroscopy coupled with site-specific nitroxide spin labeling can determine motional parameters and measure the distances between spin labels separated from 8 to 70 Å.

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