Conformational study of a collagen peptide by H-1 NMR spectroscopy: observation of the N-14-H-1 spin-spin coupling of the Arg guanidinium moiety in the triple-helix structure (Articolo in rivista)

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Label
  • Conformational study of a collagen peptide by H-1 NMR spectroscopy: observation of the N-14-H-1 spin-spin coupling of the Arg guanidinium moiety in the triple-helix structure (Articolo in rivista) (literal)
Anno
  • 1998-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/S0014-5793(98)01125-9 (literal)
Alternative label
  • Consonni, R; Santomo, L; Tenni, R; Longhi, R; Zetta, L (1998)
    Conformational study of a collagen peptide by H-1 NMR spectroscopy: observation of the N-14-H-1 spin-spin coupling of the Arg guanidinium moiety in the triple-helix structure
    in FEBS letters (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Consonni, R; Santomo, L; Tenni, R; Longhi, R; Zetta, L (literal)
Pagina inizio
  • 243 (literal)
Pagina fine
  • 246 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://ac.els-cdn.com/S0014579398011259/1-s2.0-S0014579398011259-main.pdf?_tid=ba158294-7691-11e2-bd68-00000aab0f01&acdnat=1360838083_97d94a70d8f00c287ff40a44ebca5e1b (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 436 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Consonni, R; Santomo, L; Zetta, L ISMAC Milano Longhi, R; ICRM MIlano (literal)
Titolo
  • Conformational study of a collagen peptide by H-1 NMR spectroscopy: observation of the N-14-H-1 spin-spin coupling of the Arg guanidinium moiety in the triple-helix structure (literal)
Abstract
  • CB2, a CNBr peptide of 36 residues from type I collagen alpha 1(I) chain has been studied by NMR spectroscopy as a function of temperature. At low temperature, the guanidinium protons of Arg(9) showed sharp 1:1:1 NMR triplets around 6.95 ppm, characteristic of N-14 coupled protons ((1)J(NH) = 52 Hz) when the quadrupolar relaxation rate is drastically reduced. These spectral characteristics and the low temperature coefficient of the 1:1:1 triplets (Delta delta/Delta T of -3.6 ppb/degrees C) suggest that the H atoms of the protonated guanidinium moiety of Arg(9) in the triple helix are slowly exchanging with bulk water, most likely involved in hydrogen bonds. On the basis of conformational energy computations on a model segment of type I collagen (Vitagliano, L., Nemethy, G., Zagari, A. and Scheraga, H.A. (1993) Biochemistry 32, 7354-7359), similar to CB2, our data could indicate that the guanidinium group of Arg(9) form hydrogen bonds with a backbone carbonyl of an adjacent chain probably by using the N-epsilon hydrogen, leaving the four N-eta hydrogens bound to water molecules that must be in slow exchange with bulk water and that could therefore be considered structural elements of the trimeric alpha 1(I) CB2 triple helix, The behaviour of Arg(9) has been investigated also in terms of equilibrium between random monomer and helical trimer conformations controlled by temperature, The thermal unfolding process was found to be reversible and the melting point resulted to be 17 degrees C. (literal)
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