Gas phase folding of an (Ala)4 neutral peptide chain: spectroscopic evidence for the formation of a beta-hairpin H-bonding pattern.
IR and UV laser spectroscopy of an Ala-based 4-residue model peptide recorded under gas phase isolated conditions provides evidence for the intrinsic stability of compact folded structures resembling the extremity of a beta-hairpin, with a C(14) H-bond bridging the two ends of the chain, and enables us to assess the capabilities of new quantum chemistry techniques to account for dispersive interactions in a medium-size molecule.
Gloaguen
Eric
E
CEA, IRAMIS, Service des Photons, Atomes et Molécules, F-91191 Gif-sur-Yvette, France.
Pollet
Rodolphe
R
Piuzzi
François
F
Tardivel
Benjamin
B
Mons
Michel
M
D006860:Hydrogen Bonding; D008958:Models, Molecular; D009842:Oligopeptides / Q000032:analysis*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013055:Spectrophotometry, Infrared; D013056:Spectrophotometry, Ultraviolet
D009842:Oligopeptides; C026593:alanyl-alanyl-alanyl-alanine