title: 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.
authors.affiliation: Biostructure and Biocomputing, European Molecular Biology Laboratory, Heidelberg, Germany. blanco@EMBL-heidelberg.de
authors.forename: F
authors.initials: F
authors.lastname: Blanco
authors.forename: M
authors.initials: M
authors.lastname: Ramírez-Alvarado
authors.forename: L
authors.initials: L
authors.lastname: Serrano
mesh_terms: D002942:Circular Dichroism; D007700:Kinetics; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides