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Structural model of vinculin: correlation of amino acid sequence with electron-microscopical shape

Beck, Konrad 1989. Structural model of vinculin: correlation of amino acid sequence with electron-microscopical shape. FEBS Letters 249 (1) , pp. 1-4. 10.1016/0014-5793(89)80002-X

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Abstract

The cytoskeleton-associated protein vinculin exhibits the shape of a 'balloon on a string' when examined by rotary shadowing electron microscopy. Recently, the complete primary structure of chicken vinculin was determined which leads to the questions as to whether the globule might be either hollow or disc shaped, or whether the electron micrographs resemble those of vinculin dimers. Based on a hydrodynamical theory, evidence is presented for the assumption that vinculin as a monomer consists of a compact spherical head 6 nm in diameter connected by a proline-rich domain to a rod-shaped tail about 20 nm in length.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Dentistry
Subjects: Q Science > QD Chemistry
Uncontrolled Keywords: Cytoskeleton; Electron microscopy; Protein structure; Hydrodynamics; Cell adhesion
Publisher: Elsevier
ISSN: 0014-5793
Last Modified: 04 Jun 2017 03:04
URI: http://orca.cf.ac.uk/id/eprint/16320

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