title: The twists and turns of beta-peptides.
abstract: Recently, it has been discovered that peptides composed of beta-amino acids are capable of adopting novel secondary structures demonstrating that peptides composed of alpha-amino acids are not unique in their ability to fold into well-defined structures. Cyclic as well as acyclic peptides composed of beta-amino acid residues adopt turn, helical, and sheet-like conformations. Here, we discuss the synthesis and conformational preferences of individual, substituted beta-amino acids as well as the structures that peptides composed of these residues, beta-peptides, may adopt.
authors.affiliation: Department of Biochemistry and Biophysics, Johnson Research Foundation, School of Medicine, The University of Pennsylvania, Philadelphia 19104-6059, USA.
authors.forename: W F
authors.initials: WF
authors.lastname: DeGrado
authors.forename: J P
authors.initials: JP
authors.lastname: Schneider
authors.forename: Y
authors.initials: Y
authors.lastname: Hamuro
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D009682:Magnetic Resonance Spectroscopy; D008961:Models, Structural; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods; D017433:Protein Structure, Secondary
chemical_list: D000596:Amino Acids; D010455:Peptides