Infrared spectroscopy has long been used to determine structural descriptions of proteins in a variety of static and time resolved experiments.  Our work focuses on developing new infrared methods to compare the structure, dynamics and function of nearly identical biopharmaceutical proteins.  We have developed an order parameter describing protein conformation variations around the average molecular values.  Our order parameter is applied to the problem of characterizing protein structure, function and aggregation in different environments.  By relating our order parameter and amide hydrogen/deuterium exchange stabiltiy methods, we explore the relationship between protein stability and the dynamics of the protein conformational distribution.  Examples include lysozyme and albumin in solution, and cytochrome c interacting with lipid membranes of varying net-negative surface charge density.  We have recently extended our work to the characterization of both bacteriorhodopsin during its photocycle and amyloid beta during aggregation.

Measuring protein dynamics and aggregation using infrared spectroscopy

247th National Meeting (2014)

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