title: A study of a Calpha,beta-didehydroalanine homo-oligopeptide series in the solid-state by 13C cross-polarization magic angle spinning NMR.
abstract: The fully extended peptide conformation (2.0(5)-helix) has been investigated for the first time in the solid-state by 13C cross-polarization magic angle spinning NMR. The compounds examined are members of a terminally protected, homo-oligopeptide series (from monomer through hexamer) based on Calpha,beta-didehydroalanine.
authors.affiliation: Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA.
authors.forename: Katherine A
authors.initials: KA
authors.lastname: Henzler Wildman
authors.forename: Ayyalusamy
authors.initials: A
authors.lastname: Ramamoorthy
authors.forename: Tateaki
authors.initials: T
authors.lastname: Wakamiya
authors.forename: Taichi
authors.initials: T
authors.lastname: Yoshikawa
authors.forename: Marco
authors.initials: M
authors.lastname: Crisma
authors.forename: Claudio
authors.initials: C
authors.lastname: Toniolo
authors.forename: Fernando
authors.initials: F
authors.lastname: Formaggio
mesh_terms: D000409:Alanine / Q000737:chemistry*; D002247:Carbon Isotopes; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D002247:Carbon Isotopes; D009842:Oligopeptides; D000409:Alanine