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An electron microscopic and optical diffraction analysis of the structure of Limulus telson muscle thick filaments

Long, thick filaments (greater than 4.0 micrometer) rapidly and gently isolated from fresh, unstimulated Limulus muscle by an improved procedure have been examined by electron microscopy and optical diffraction. Images of negatively stained filaments appear highly periodic with a well-preserved myos...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1982
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112063/
https://www.ncbi.nlm.nih.gov/pubmed/7199531
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collection PubMed
description Long, thick filaments (greater than 4.0 micrometer) rapidly and gently isolated from fresh, unstimulated Limulus muscle by an improved procedure have been examined by electron microscopy and optical diffraction. Images of negatively stained filaments appear highly periodic with a well-preserved myosin cross-bridge array. Optical diffraction patterns of the electron micrographs show a wealth of detail and are consistent with a myosin helical repeat of 43.8 nm, similar to that observed by x-ray diffraction. Analysis of the optical diffraction patterns, in conjunction with the appearance in electron micrographs of the filaments, supports a model for the filament in which the myosin cross-bridges are arranged on a four-stranded helix, with 12 cross-bridges per turn or each helix, thus giving an axial repeat every third level of cross-bridges (43.8 nm).
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spelling pubmed-21120632008-05-01 An electron microscopic and optical diffraction analysis of the structure of Limulus telson muscle thick filaments J Cell Biol Articles Long, thick filaments (greater than 4.0 micrometer) rapidly and gently isolated from fresh, unstimulated Limulus muscle by an improved procedure have been examined by electron microscopy and optical diffraction. Images of negatively stained filaments appear highly periodic with a well-preserved myosin cross-bridge array. Optical diffraction patterns of the electron micrographs show a wealth of detail and are consistent with a myosin helical repeat of 43.8 nm, similar to that observed by x-ray diffraction. Analysis of the optical diffraction patterns, in conjunction with the appearance in electron micrographs of the filaments, supports a model for the filament in which the myosin cross-bridges are arranged on a four-stranded helix, with 12 cross-bridges per turn or each helix, thus giving an axial repeat every third level of cross-bridges (43.8 nm). The Rockefeller University Press 1982-02-01 /pmc/articles/PMC2112063/ /pubmed/7199531 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
An electron microscopic and optical diffraction analysis of the structure of Limulus telson muscle thick filaments
title An electron microscopic and optical diffraction analysis of the structure of Limulus telson muscle thick filaments
title_full An electron microscopic and optical diffraction analysis of the structure of Limulus telson muscle thick filaments
title_fullStr An electron microscopic and optical diffraction analysis of the structure of Limulus telson muscle thick filaments
title_full_unstemmed An electron microscopic and optical diffraction analysis of the structure of Limulus telson muscle thick filaments
title_short An electron microscopic and optical diffraction analysis of the structure of Limulus telson muscle thick filaments
title_sort electron microscopic and optical diffraction analysis of the structure of limulus telson muscle thick filaments
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112063/
https://www.ncbi.nlm.nih.gov/pubmed/7199531