Structural studies of synthetic filaments prepared from column-purified myosin.

Abstract:

:Synthetic filaments prepared from column-purified rabbit skeletal myosin by slow dialysis exhibit characteristic bipolar organization and 14-nm axial subunit spacing. Backbone substructure can be discerned in high resolution micrographs in the form of striations of 3--4-nm width and slight angular tilt from the direction of the filament axis. Filament backbone diameters vary over the population, although remaining relatively constant for a single filament. Approximately 25% of the filaments appear poorly stained and frayed, which may be due to collapse on the electron microscope grid. Optical diffraction studies reveal a 43-nm axial repeat as well as the 14.3-nm subunit repeat, indicating a structural homology with natural filaments. A model for synthetic filament aggregation is presented that is consistent with observations of backbone diameter variation, absence of bare zones, and the presence of fraying filaments.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Koretz JF

doi

10.1016/S0006-3495(79)85226-1

subject

Has Abstract

pub_date

1979-09-01 00:00:00

pages

423-32

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(79)85226-1

journal_volume

27

pub_type

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