Elastin structures and their significance towards elastic recoil properties
have been reviewed. Starting from the initial hypothesis that elastin conf
ormation is conditioned by that of its monomer, the structure of tropoelast
in was first described using theoretical and experimental methods and a bet
a class folding type was evidenced for the isolated unbound tropoelastin mo
lecules. The structure of elastin in the solid state was consistent with th
at of its monomer and consequently, fibrous elastin appeared constituted of
globular tropoelastin molecules. Finally, theoretical and experimental con
siderations have led us to the conclusion that the functional form of the e
lastomer, water swollen elastin, could be a triphasic system comprising the
protein chains, hydration water and solvent water. Following this descript
ion, the dynamic structural equilibria occurring within elastin hydrophobic
domains and the plastisizing effect of water could explain elastin elastic
ity, in keeping with a classical entropic mechanism. (C) 1999 Societe franc
aise de biochimie et biologie moleculaire / Editions scientifiques et medic
ales Elsevier SAS.