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Issue 40, 2006
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Study of conformational properties of a biologically active peptide of fibronectin by circular dichroism, NMR and molecular dynamics simulation

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Abstract

Circular dichroism (CD), and NMR spectra have been recorded and molecular dynamics (MD) simulations have been performed in water and watertrifluoroethanol (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. 1H-NOE data were found to be consistent with the most abundant calculated conformation.

Graphical abstract: Study of conformational properties of a biologically active peptide of fibronectin by circular dichroism, NMR and molecular dynamics simulation

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Supplementary files

Article information


Submitted
04 Apr 2006
Accepted
04 Sep 2006
First published
19 Sep 2006

Phys. Chem. Chem. Phys., 2006,8, 4668-4677
Article type
Paper

Study of conformational properties of a biologically active peptide of fibronectin by circular dichroism, NMR and molecular dynamics simulation

S. Abbate, S. Barlati, M. Colombi, S. L. Fornili, P. Francescato, F. Gangemi, F. Lebon, G. Longhi, P. Manitto, T. Recca, G. Speranza and N. Zoppi, Phys. Chem. Chem. Phys., 2006, 8, 4668
DOI: 10.1039/B604807B

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