Conformational and Structural Analysis of the Equilibrium Between Simple and Double Strand beta-Helix of a D,L-Alternating Oligonorleucine (Articolo in rivista)

Type
Label
  • Conformational and Structural Analysis of the Equilibrium Between Simple and Double Strand beta-Helix of a D,L-Alternating Oligonorleucine (Articolo in rivista) (literal)
Anno
  • 2004-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002bip.10549 (literal)
Alternative label
  • Fenude E., Navarro E., Celda B., (2004)
    Conformational and Structural Analysis of the Equilibrium Between Simple and Double Strand beta-Helix of a D,L-Alternating Oligonorleucine
    in Biopolymers (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Fenude E., Navarro E., Celda B., (literal)
Pagina inizio
  • 229 (literal)
Pagina fine
  • 241 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • I.F. 3.99 (Biopolymers 2004); N.C. 23 (al 16/10/2013). La struttura del composto HCO-(D-Nle-L-Nle)3-D-MeNle-L-Nle-D-Nle-L-Nle-OMe, oggetto dell'articolo è stata pubblicata su RCSB Protein Data Bank, classificata con la sigla 1S4A. (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 73 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 13 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Dipartimento di Chimica Fisica, facoltà di Chimica, Università di Valenzia (Spagna), Istituto di Chimica Biomolecolare -CNR -Sassari (literal)
Titolo
  • Conformational and Structural Analysis of the Equilibrium Between Simple and Double Strand beta-Helix of a D,L-Alternating Oligonorleucine (literal)
Abstract
  • RCSB Protein Data Bank, NMR Structure of a D,L alternating decamer of norleucine: double antiparallel beta-helix HCO-(D-Nle-L-Nle)3-D-MeNle-L-Nle-D-Nle-L-Nle-OMe Compound-1S4A (literal)
  • Alternating sequences of D and L residues in peptides are directly related to the formation of several kinds of regular helical conformations usually called ?-helices. The major feature of these structures is that they can be associated with the transmembrane ion-conducting channel activity in some natural antibacterial peptides. The study of alternating D,L synthetic peptides is critical to understand how factors such as surrounding media, main chain length, type of side chain and terminal groups, among others, can determine the adoption of a specific kind of ?-helix. The influence of terminal groups on the final stable conformation of Nformylated peptides has been studied in this work. The initial basic NMR data analysis of a synthetic alternating D,L-oligopeptide with ten norleucines, N-methylated on the residue 7 and having HCO-- and --OMe as terminal groups clearly indicates the coexistence of two different conformations in equilibrium. NMR data and molecular dynamics calculations point to a dimeric antiparallel ?-helix structure ?for the main conformation. On the other hand, NMR data suggest a single ?-helix structure for the second conformation. Finally, a thermodynamic analysis of the equilibrium between both conformations has been carried out by one-dimensional NMR measurements at ten different temperatures. The temperature at which 50% of dimer conformation is dissociated is 319. (literal)
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