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Structure of short thick filaments from Limulus muscle.

Abstract：

:Shortened Limulus thick filaments, isolated from stimulated muscle, are structurally similar to long filaments, isolated from unstimulated muscle, except for length. Both have 3-fold screw symmetry with a helical repeat at approximately 43 nm, axial spacing of 14.5 nm between successive crowns of crossbridges and 4-fold rotational symmetry as estimated from the Bessel argument, by analysis of optical transforms of electron micrograph negatives of negatively stained samples. Both short and long filaments also have similar radii for the location of their crossbridges, thus similar diameters. Equal numbers of subunits/helical strand are also apparent on images of metal-shadowed long and short filaments. Since these data argue against molecular reorganization during filament shortening, it is suggested that the change in length of Limulus thick filaments may occur by reversible disaggregation of constituent protein molecules.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Levine RJ,Kensler RW

doi

10.1016/0022-2836(85)90351-1

subject

Has Abstract

pub_date

1985-03-20 00:00:00

pages

347-52

issue

2

eissn

0022-2836

issn

1089-8638

pii

0022-2836(85)90351-1

journal_volume

182

pub_type

杂志文章

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