@article{2959260,
    title = "“Glass transition” in peptides: Temperature and pressure effects",
    author = "P. Papadopoulos and G. Floudas and I. Schnell and H.-A. Klok and T. Aliferis and H. Iatrou and N. Hadjichristidis",
    journal = "The Journal of Chemical Physics",
    year = "2005",
    volume = "122",
    number = "22",
    pages = "224906",
    publisher = "AIP Publishing",
    doi = "10.1063/1.1931657",
    keywords = "Glass-forming liquids;  Peptides;  Secondary structures;  Thermal energy, Amino acids;  Biopolymers;  Conformations;  Fourier transform infrared spectroscopy;  Molecular structure;  Nuclear magnetic resonance;  Polymerization;  Pressure effects;  Temperature distribution, Glass transition",
    abstract = "We report on the origin of the liquid-to-glass transition in a series of oligopeptides of γ -benzyl- L -glutamate up to the polymer (PBLG), and in Poly- Z - L -lysine (PZLL) and Polyglycine (PGly) using dielectric spectroscopy as a function of temperature and pressure. We show that temperature is the dominant control variable of the dynamics associated with the peptidic "glass transition." This is an intrinsic feature of the peptide dynamics, irrespective of the type of amino acid and of the peptide secondary structure. The influence of the type of secondary structure (α helix vs Β sheet) on the liquid-to-glass dynamics is discussed. © 2005 American Institute of Physics."
}