RUI: Effects of Solvent-backbone Hydrogen Bonding and Backbone N-methylation on Peptide Conformation

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The role of water-backbone interactions in stabilizing peptide conformation has become an exciting area of study, both by computational and experimental approaches. This project will build upon the PI''s previous work on the development of isotope-edited infrared techniques by taking four different approaches to the study of backbone-water hydrogen bonding: (1) the effects of high pressure on solvent-backbone interactions; (2) backbone dehydration by helix-promoting fluorinated co-solvents; (3) selective backbone dehydration in helices by side-chain shielding effects; and (4) conformation and solvation of N-methylated peptides.All of the work in this project will be carried out with undergraduate women who are students at Mount Holyoke College. The research experience gained will be important to the training of many new scientists. In the past 12 years, the PI has worked with 55 undergraduate researchers. Fifteen of these are currently enrolled or have completed Ph.D. programs in chemistry or related fields. This project is being jointly supported by Molecular Biophysics in the Division of Molecular and Cellular Biosciences and the Experimental Physical Chemistry Program in the Chemistry Division.