Document Detail


Optical diffraction of tropoelastin and alpha-elastin coacervates.
MedLine Citation:
PMID:  952955     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
D Volpin; D W Urry; B A Cox; L Gotte
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  439     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1976 Jul 
Date Detail:
Created Date:  1976-10-29     Completed Date:  1976-10-29     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  253-8     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Elastin*
Macromolecular Substances
Protein Binding
Protein Conformation
Protein Precursors*
Spectrum Analysis
X-Ray Diffraction
Chemical
Reg. No./Substance:
0/Macromolecular Substances; 0/Protein Precursors; 9007-58-3/Elastin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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