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Characterization of low populated peptide helical structures in solution by means of NMR proton conformational shifts

Autor
Bruix, M.; Perello, M.; Herranz, J.; Ríco, M.
Tipus d'activitat
Article en revista
Revista
Biochemical and biophysical research communications
Data de publicació
1990-03
Volum
0
Número
167
Pàgina inicial
1009
Pàgina final
1014
DOI
https://doi.org/10.1016/0006-291X(90)90623-U Obrir en finestra nova
Resum
A NOE independent NMR method is proposed to characterize unambiguosly residues involved in low populated isolated peptide helices. The method is based on the comparison of amide and Ha chemical shift changes originated upon the addition of stabilizing or denaturing agents with true helical conformational shifts that have been measured for the first time using an isolated model peptide helix, the one formed by Ac-(Leu-Lys-Lys-Leu)3-NHEt in aqueous solution.

Participants

  • Bruix, Marta  (autor)
  • Perello Cuart, Margarita  (autor)
  • Herranz, José  (autor)
  • Ríco Secades, Manuel  (autor)