A protein's chemical properties and biological activities depend on its functional groups as well as its shape and structure.  In order to better understand the relationship between the structure and activity of proteins we chose to characterize dipeptide molecules.  There are 400 possible combinations of dipeptides that could be coupled from the 20 naturally occurring L-amino acids.  Most of these permutations are part of protein sequences, but a large number of dipeptides also occur independently in nature, with many of them being physiologically interesting.  Research on dipeptides yields information on the characteristics of larger proteins, as well as to operate as a base on which to begin more intensive research into pharmacologically active dipeptides and their variations.  We plan to present structure determination in the solid and solution states as well as FTIR, and Raman spectroscopic characterization and compare the results with predicted structures and properties from energy minimization.  Our student will showcase the skills they acquired during an NSF-funded research internship; notably in using NMR, FTIR, and Raman spectroscopy, as well as single-crystal X-ray diffraction in the characterization of selected dipeptides.

Characterization of dipeptides as a means to understand larger proteins: The result of intensive, hands-on laboratory training

241st National Meeting (2011)

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