Hydrogen/deuterium exchange studies of short, helical peptides in nonaqueous solvents

CHED 339

Melissa Guildford, mkubasik@mail.fairfield.edu and Matthew Kubasik, mkubasik@mail.fairfield.edu. Department of Chemistry, Fairfield University, 1073 N. Benson Rd, Fairfield, CT 06824
We have performed hydrogen/deuterium (H/D) exchange studies on a series of short oligomers of α-aminoisobutyric acid (Aib). The Aib residue has two α-methyl groups which restrict the conformation of the residue to a small region of the Ramachandran map characterizing two types of helical structures, α helices and 310 helices. Small differences in φ, ψ angles for residues in these two types of helices result in distinct intramolecular hydrogen bonding patterns: i/i+3 for the 310 helix and i/i+4 for the α helix. These hydrogen bonding patterns may be distinguished by H/D exchange studies. Results for tetramers and octamers of Aib with varying C-terminal protecting groups implicated in the α/310 helix equilibrium will be discussed.
 

Undergraduate Research Poster Session
2:30 PM-4:30 PM, Monday, August 20, 2007 BCEC -- Exhibit Hall - B2, Poster

Division of Chemical Education

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007