Formation and stability of beta-hairpin structures in polypeptides

Abstract

Experimental work on peptide models with beta-hairpin structures has provided new insights into the formation and stability of this secondary structure element. Both the turn region and the antiparallel strand residues not only affect the overall stability of the hairpin, but also determine the type of hairpin formed. These results agree reasonably well with those from experimental and statistical analyses of beta-sheet structures in proteins.