Optical diffraction of tropoelastin and alpha-elastin coacervates.

D Volpin; D W Urry; B A Cox; L Gotte

doi:10.1016/0005-2795(76)90181-1

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Optical diffraction of tropoelastin and alpha-elastin coacervates.

D Volpin·D W Urry·B A Cox·L Gotte

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Abstract

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.

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Elastin Macromolecular Substances Protein Binding Protein Conformation Protein Precursors Spectrum Analysis X-Ray Diffraction Journal Article Research Support, U.S. Gov't, P.H.S.

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D Volpin, D W Urry, B A Cox, L Gotte. 1976-07-19. Optical diffraction of tropoelastin and alpha-elastin coacervates.. https://doi.org/10.1016/0005-2795(76)90181-1

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