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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Journal of Muscle Re...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Journal of Muscle Research and Cell Motility
Article . 1988 . Peer-reviewed
License: Springer TDM
Data sources: Crossref
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Structure of tropomyosin-troponin T cocrystals

Authors: H J, Carr; E J, O'Brien; E P, Morris;

Structure of tropomyosin-troponin T cocrystals

Abstract

Crystals formed from a mixture of tropomyosin and troponin T have an open double-stranded lattice structure with a diamond-shaped repeat. In some regions the appearance in electron micrographs of negatively stained specimens changes from this double-diamond lattice to a more condensed banded crystal form. The double-diamond lattice has plane group symmetry cmm with unit cell 76.3 by 21.7 nm. The molecules form continuous chains along the diagonal of the unit cell and the diagonal length (79.4 nm) is that expected for two tropomyosin molecules joined end-to-end. Computer filtering of the micrographs shows that the strands of the lattice are thicker from the acute vertex of the large diamond to a point about half-way along the side of the diamond, where there is a small blob of density. At the acute vertex of the diamond is a large blob of density which is accentuated, however, by being at the lattice node where strands cross each other, and which is much weaker in regions of the micrographs where the crystals have condensed laterally. The results indicate that troponin T is a long thin molecule running in contact with the tropomyosin strands over 40-50% of the tropomyosin molecular length. The small globular region may represent the end-to-end overlap of tropomyosin but is more likely to be a globular region at the C-terminal region of troponin T.

Related Organizations
Keywords

Chemistry, Microscopy, Electron, Chemical Phenomena, Muscles, Image Processing, Computer-Assisted, Animals, Rabbits, Tropomyosin, Crystallization, Troponin

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
9
Average
Top 10%
Average
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