Solvation and Hydrogen Bonding in Alanine- and Glycine-Containing Dipeptides Probed Using Solutionand Solid-State NMR Spectroscopy
The NMR chemical shift is a sensitive reporter of peptide secondary structure and its solvation environment, and it is potentially rich with information about both backbone dihedral angles and hydrogen bonding. We report results from solution- and solid-state 13C and 15N NMR studies of four zwitterionic model dipeptides, l-alanyl-l-alanine, l-alanyl-glycine, glycyl-l-alanine, and glycyl-glycine, in which we attempt to isolate structural and environmental contributions to the chemical shift. We have mapped hydrogen-bonding patterns in the crystalline states of these dipeptides using the published crystal structures and correlated them with 13C and 15N magic angle spinning chemical shift data. To aid in the interpretation of the solvated chemical shifts, we performed ab initio quantum chemical calculations to determine the low-energy conformers and their chemical shifts. Assuming low energy barriers to interconversion between thermally accessible conformers, we compare the Boltzmann-averaged chemical shifts with the experimentally determined solvated-state shifts. The results allow us to correlate the observed differences in chemical shifts between the crystalline and solvated states to changes in conformation and hydrogen bonding that occur upon solvation.
Bhate, Manasi P., Jaie C. Woodard, and Manish A. Mehta. 2009. "Solvation and Hydrogen Bonding in Alanine- and Glycine-Containing Dipeptides Probed Using Solutionand Solid-State NMR Spectroscopy." Journal Of The American Chemical Society 131(27): 9579-9589.
American Chemical Society
Journal of the American Chemical Society
Chemistry and Biochemistry