Phase transitions and chain dynamics, in the solid state, of a pentapeptide sequence of elastins.
Differential scanning calorimetry (d.s.c.) and thermally stimulated current (t.s.c.) have been applied to the study of thermal transitions and dielectric relaxations of a pentapeptide sequence: Gly-Leu-Gly-Gly-Val of elastin. The manifestation of the glass transition has been observed by both techniques. The analysis of the fine structure of t.s.c. spectra reveals the existence of local order in the amorphous phase upon physical ageing. In the 'true' amorphous phase, cooperative motions of sequences of various length are observed. The corresponding activation parameters are characteristic of the 'structure' of the amorphous phase and might be used as reference for further studies.
Megret
C
C
Pierre Fabre Médicaments, Castres, France.
Guantieri
V
V
Lamure
A
A
Pieraggi
M T
MT
Lacabanne
C
C
Tamburro
A M
AM
D000595:Amino Acid Sequence; D002152:Calorimetry, Differential Scanning / Q000379:methods; D004549:Elastin / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation
D009842:Oligopeptides; D004549:Elastin