Helical folding and unfolding can be induced by changes in the environment of model peptides and natural-sequence proteins. The formation of the helical structure is accompanied by substantial changes in the solvent and speciation around a sequence that folds or unfolds.  Vibrationally labeled amino acid side chains containing the thiocyanato and azido functional groups can report on differences in the solvation around selected sites.  Studies in model peptides, peptides that bind to proteins, and proteins that bind to lipids all exhibit site-specific changes in the composition and the dynamics of the solvent species closest to the labeled residues of interest.  Examples from model peptides and the protein calmodulin and its physiological binding partners will be discussed.

Changes in the solvent around helical structures are reflected by vibrations on artificial amino acid side chains

244th National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.