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Gas-phase models of γ turns: Effect of side-chain/backbone interactions investigated by IR/UV spectroscopy and quantum chemistry

Chin, Wutharath ; Piuzzi, François ; Dognon, Jean-Pierre ; Dimicoli, Iliana ; Mons, Michel

The Journal of chemical physics, 2005-08, Vol.123 (8), p.084301-084301-11 [Periódico revisado por pares]

United States: American Institute of Physics

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Título:
Gas-phase models of γ turns: Effect of side-chain/backbone interactions investigated by IR/UV spectroscopy and quantum chemistry
Autor: Chin, Wutharath ; Piuzzi, François ; Dognon, Jean-Pierre ; Dimicoli, Iliana ; Mons, Michel
Assuntos: Alanine - chemistry ; Amino Acid Motifs ; Chemical Sciences ; Chemistry, Physical - methods ; Hydrogen Bonding ; Models, Chemical ; Models, Molecular ; Molecular Conformation ; or physical chemistry ; Peptides - chemistry ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Quantum Theory ; Spectrophotometry ; Spectrophotometry, Infrared - methods ; Spectrophotometry, Ultraviolet - methods ; Theoretical and ; Valine - chemistry
É parte de: The Journal of chemical physics, 2005-08, Vol.123 (8), p.084301-084301-11
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: The conformations of laser-desorbed jet-cooled short peptide chains Ac - Phe - Xxx - N H 2 ( Xxx = Gly , Ala, Val, and Pro) have been investigated by IR/UV double resonance spectroscopy and density-functional-theory (DFT) quantum chemistry calculations. Singly γ -folded backbone conformations ( β L - γ ) 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 ( β L for Phe and γ turn for Xxx). Besides, β 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 γ turns. In the case of valine, two similar types of γ 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 - N H 2 is also discussed.
Editor: United States: American Institute of Physics
Idioma: Inglês

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Gas-phase models of γ turns: Effect of side-chain/backbone interactions investigated by IR/UV spectroscopy and quantum chemistry

Chin, Wutharath ; Piuzzi, François ; Dognon, Jean-Pierre ; Dimicoli, Iliana ; Mons, Michel

United States: American Institute of Physics

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