Dr. Baldwin will continue his investigation of the stabilization forces of short helical peptides. He has previously shown that short peptides are able to form monomeric -helices in aqueous solution. Helical stability depended strongly on residue spacing in this set of peptides and therefore helix stabilization by salt bridges was likely. He will now extend this study to include other pairs of charged residues potentially able to form salt bridges in order to evaluate the helix-stabilizing properties of these salt bridges, if they exist, and to investigate further the mechanism of -helix stabilization by salt bridges and non-H- bonded ion pairs. Salt bridges formed by short helices of de novo design are being studied by only a few scientists. The study of designed helices is closely related to the study of -helix formation by naturally occurring peptides derived from helix- containing segments of peoteins. The broad significance of this work is that short helices, formed at early stages in the folding process, have the ability to play a directing role in the pathway of protein folding.***//
