Study of conformational properties of a biologically active peptide of fibronectin by circular dichroism, NMR and molecular dynamics simulation.
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.
Abbate
Sergio
S
Dipartimento di Scienze Biomediche e Biotecnologie, Università di Brescia, viale Europa 11, 25123 Brescia, Italy. abbate@med.unibs.it
Barlati
Sergio
S
Colombi
Marina
M
Fornili
Sandro L
SL
Francescato
Pierangelo
P
Gangemi
Fabrizio
F
Lebon
France
F
Longhi
Giovanna
G
Manitto
Paolo
P
Recca
Teresa
T
Speranza
Giovanna
G
Zoppi
Nicoletta
N
D002942:Circular Dichroism / Q000379:methods; D003198:Computer Simulation; D005353:Fibronectins / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry*; D014867:Water / Q000737:chemistry
D005353:Fibronectins; D010455:Peptides; D014867:Water