@article{2959230,
    title = "Control of peptide secondary structure and dynamics in poly(γ-benzyl- L-glutamate)-b-polyalanine peptides",
    author = "A. Gitsas and G. Floudas and M. Mondeshki and H. W. Spiess and T. Aliferis and H. Iatrou and N. Hadjichristidis",
    journal = "Macromolecules",
    year = "2008",
    volume = "41",
    number = "21",
    pages = "8072--8080",
    publisher = "American Chemical Society (ACS)",
    issn = "0024-9297, 1520-5835",
    doi = "10.1021/ma801770b",
    keywords = "Dielectric spectroscopy;  Dynamics;  Electron energy levels;  Nuclear magnetic resonance;  Nuclear magnetic resonance spectroscopy;  Polypeptides, Enthalpic interactions;  Helicity;  Nanophase separations;  Peptide secondary structures;  Polyalanine;  Polyalanine peptides;  Time scales, Amines",
    abstract = "The stability, persistence and dynamics of the peptide secondary motifs are investigated in a series of poly(γ-benzyl-L-glutamate)-b-polyalanine (PBLG-b-PAla) polypeptides through a combination of structural (X-rays, NMR) and dynamic (Dielectric Spectroscopy, NMR) probes. The unfavorable enthalpic interactions between the unlike blocks give rise to nanophase separation that results in the destabilization of PAla β-sheets. Contrary to this, the overall helicity of PBLG α-helices is enhanced. The dynamics of the "defected" amorphous segments and of the more ordered segments are studied by DS and 13C NMR, respectively. These probes provide information on the time scale and the mechanism of molecular and supramolecular motion. © 2008 American Chemical Society."
}