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  • Title: Study of conformational properties of a biologically active peptide of fibronectin by circular dichroism, NMR and molecular dynamics simulation.
    Author: Abbate S, Barlati S, Colombi M, Fornili SL, Francescato P, Gangemi F, Lebon F, Longhi G, Manitto P, Recca T, Speranza G, Zoppi N.
    Journal: Phys Chem Chem Phys; 2006 Oct 28; 8(40):4668-77. PubMed ID: 17047765.
    Abstract:
    Circular dichroism (CD), and NMR spectra have been recorded and molecular dynamics (MD) simulations have been performed in water and water-trifluoroethanol (TFE) mixed solvent for a synthetic biologically active 13-amino-acid fragment of human fibronectin and two related peptides. The CD results are interpreted on the basis of statistical analyses of MD trajectories and of ensuing calculations of CD spectra based on Schellman's matrix method. It is observed that the peptide conformation is quite variable in water and loses its mobility with the addition of TFE. (1)H-NOE data were found to be consistent with the most abundant calculated conformation.
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