skip to main content
Idioma:
Primo Search
Clear Search Box
Search in: Busca Geral
Busca Avançada
Busca por Índices
Tipo de recurso Mostra resultados com: Mostra resultados com: Índice

Probing the competition between secondary structures and local preferences in gas phase isolated peptide backbones

CHIN, Wutharath ; PIUZZI, Francois ; DIMICOLI, Iliana ; MONS, Michel

Physical chemistry chemical physics : PCCP, 2006-01, Vol.8 (9), p.1033-1048 [Periódico revisado por pares]

Cambridge: Royal Society of Chemistry

Texto completo disponível

Citações Citado por
  • Título:
    Probing the competition between secondary structures and local preferences in gas phase isolated peptide backbones
  • Autor: CHIN, Wutharath ; PIUZZI, Francois ; DIMICOLI, Iliana ; MONS, Michel
  • Assuntos: Chemical Sciences ; Chemistry ; Dipeptides - chemistry ; Exact sciences and technology ; General and physical chemistry ; Hydrogen Bonding ; Models, Molecular ; Molecular Conformation ; Oligopeptides - chemistry ; or physical chemistry ; Protein Structure, Secondary ; Spectrophotometry, Infrared ; Spectrophotometry, Ultraviolet ; Theoretical and
  • É parte de: Physical chemistry chemical physics : PCCP, 2006-01, Vol.8 (9), p.1033-1048
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
  • Descrição: Combining laser desorption with a supersonic expansion together with the selectivity of IR/UV double resonance spectroscopy makes it possible to isolate and characterise the gas phase of remarkable backbone conformations of short peptide chains mimicking protein segments. A systematic bottom-up approach involving a conformer-specific IR study of peptide sequences of increasing sizes has enabled us to map the spectral signatures of the intramolecular interactions, which shape the peptide backbone, in particular H-bonds. The precise data collected are directly comparable to the most sophisticated quantum chemistry calculations of these species and therefore constitute a stringent test for the theoretical methods used. One-residue chains reveal the local conformational preference of the backbone and its dependence upon the nature of the residue. The investigation of longer chains provides evidence for a competition between simple successions of local conformational preferences along the chain and more folded structures, in which a new H-bonding network, involving distant H-bonding sites along the backbone, takes place. From three residues, the issue of helical folding can also be addressed. The present review of the gas phase literature data emphasizes the observation of remarkable secondary structures of biology, including short segments of beta-strands, gamma- and beta-turns, combinations of turns, including a 3(10) helix. It also provides evidence for the flexibility of the peptide chains, i.e., a critical influence of rather minor interactions (like side-chain/backbone interactions) on the conformational stability. Finally, the paper will discuss future promising directions of the present approach.
  • Editor: Cambridge: Royal Society of Chemistry
  • Idioma: Inglês
Links
Voltar para lista de resultados

  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

Buscando em bases de dados remotas. Favor aguardar.