Optical diffraction of tropoelastin and alpha-elastin coacervates.
Optical diffraction applied to micrographs of coacervated tropoelastin and alpha-elastin show an equatorial repeat around 50 A. This confirms a 50 A center-to-center distance of parallel aligned filaments to be a fundamental property of the tropoelastin and alpha-elastin coacervates. This periodicity is similar to that of mature cross-linked elastin. These results allow the conclusion that hydrophobic association is the predominant driving force for formation of filamentous elastin in vitro. It is suggested that the coacervate is a model for relaxed fibrous elastin.
D004549:Elastin; D046911:Macromolecular Substances; D011485:Protein Binding; D011487:Protein Conformation; D011498:Protein Precursors; D013057:Spectrum Analysis; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D011498:Protein Precursors; D004549:Elastin