title: Gas-phase models of gamma turns: effect of side-chain/backbone interactions investigated by IR/UV spectroscopy and quantum chemistry.
abstract: The conformations of laser-desorbed jet-cooled short peptide chains Ac-Phe-Xxx-NH2 (Xxx=Gly, Ala, Val, and Pro) have been investigated by IR/UV double resonance spectroscopy and density-functional-theory (DFT) quantum chemistry calculations. Singly gamma-folded backbone conformations (betaL-gamma) are systematically observed as the most stable conformers, showing that in these two-residue peptide chains, the local conformational preference of each residue is retained (betaL for Phe and gamma turn for Xxx). Besides, beta turns are also spontaneously formed but appear as minor conformers. The theoretical analysis suggests negligible inter-residue interactions of the main conformers, which enables us to consider these species as good models of gamma turns. In the case of valine, two similar types of gamma turns, differing by the strength of their hydrogen bond, have been found both experimentally and theoretically. This observation provides evidence for a strong flexibility of the peptide chain, whose minimum-energy structures are controlled by side-chain/backbone interactions. The qualitative conformational difference between the present species and the reversed sequence Ac-Xxx-Phe-NH2 is also discussed.
authors.affiliation: Laboratoire Francis Perrin (URA CEA-CNRS 2453), Service des Photons, Atomes et Molécules, Centre d'Etudes de Saclay, Bâtiment 522, 91191 Gif-sur-Yvette Cedex, France. chin@drecam.cea.fr
authors.forename: Wutharath
authors.initials: W
authors.lastname: Chin
authors.forename: François
authors.initials: F
authors.lastname: Piuzzi
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Dognon
authors.forename: Iliana
authors.initials: I
authors.lastname: Dimicoli
authors.forename: Michel
authors.initials: M
authors.lastname: Mons
mesh_terms: D000409:Alanine / Q000737:chemistry; D020816:Amino Acid Motifs; D002627:Chemistry, Physical / Q000379:methods*; D006860:Hydrogen Bonding; D008956:Models, Chemical; D008958:Models, Molecular; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011789:Quantum Theory; D013053:Spectrophotometry; D013055:Spectrophotometry, Infrared / Q000379:methods*; D013056:Spectrophotometry, Ultraviolet / Q000379:methods*; D014633:Valine / Q000737:chemistry
chemical_list: D010455:Peptides; D014633:Valine; D000409:Alanine