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Science 14 March 1969:
Vol. 163. no. 3872, pp. 1196 - 1198
DOI: 10.1126/science.163.3872.1196

Articles

Paramyosin: Molecular Length and Assembly

John Kendrick-Jones 1, Carolyn Cohen 2, Andrew G. Szent-Györgyi 1, and William Longley 2

1 Department of Biology, Brandeis University, Waltham, Massachusetts 02154
2 Laboratory of Structural Molecular Biology, Children's Cancer Research Foundation, Boston, Massachusetts

Paratnyosin paracrystails formned with divalent cations have a 725-angstrom axial period and show simple negative staining patterns in the electron microscope. The structure of the aggregates is interpreted in terms of an array of polar molecules about 1275 angstroms long, with "gaps" and "overlaps" in the molecular assembly. Antiparallel relatiotns between molecules lead to the assembly of paracrystals with opposite polarity at either end. Implications of the in vitro structure for filaments containing paramyosin in muscle are discussed.


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The carboxyl-terminal isoforms of smooth muscle myosin heavy chain determine thick filament assembly properties.
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