"Glass transition" in peptides: Temperature and pressure effects
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 ß sheet) on the liquid-to-glass dynamics is discussed. © 2005 American Institute of Physics.
Keywords: Amino acids ; Biopolymers ; Conformations ; Fourier transform infrared spectroscopy ; Molecular structure ; Nuclear magnetic resonance ; Polymerization ; Pressure effects ; Temperature distribution ; Glass-forming liquids ; Peptides ; Secondary structures ; Thermal energy ; Glass transition
00219606 (ISSN), Export Date: 25 September 2007, Source: Scopus, CODEN: JCPSA, doi: 10.1063/1.1931657
Record created on 2007-10-15, modified on 2016-08-08