A study of a Calpha,beta-didehydroalanine homo-oligopeptide series in the solid-state by 13C cross-polarization magic angle spinning NMR.
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.
Henzler Wildman
Katherine A
KA
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA.
Ramamoorthy
Ayyalusamy
A
Wakamiya
Tateaki
T
Yoshikawa
Taichi
T
Crisma
Marco
M
Toniolo
Claudio
C
Formaggio
Fernando
F
D000409:Alanine / Q000737:chemistry*; D002247:Carbon Isotopes; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation
D002247:Carbon Isotopes; D009842:Oligopeptides; D000409:Alanine