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Tropomyosin: Amino Acid Sequence and Coiled-Coil Structure

Hodges, R. S., Sodek, J., Smillie, L. B., Jurasek, L.·1973·Cold Spring Harbor Symposia on Quantitative Biology

Abstract

Tropomyosin preparations of mol wt of about 70,000 daltons are known to dissociate in the presence of reducing agents and denaturing media to monomers of about 35,000 daltons (McCubbin et al., 1967; Holtzer et al., 1965; Woods, 1967, 1969; Weber and Osborne, 1969; Olander et al., 1967). The highly helical (>90%) polypeptide chains are believed to be arranged in a two-stranded coiled-coil (Crick, 1953; Cohen and Holmes, 1963) whose structure is stabilized by hydrophobic interactions between the two strands of α-helix. The relative unimportance of electrostatic interactions in the stabilization of the structure is indicated by the unusual stability of the molecule in acid and alkali (Lowey, 1965; Riddiford and Scheraga, 1962), even though the content of charged amino acid residues is remarkably high (Hodges and Smillie, 1970). In the structure proposed by Crick (1953), two α-helices are packed side-by-side in a "knobs-into-holes" manner. In order to interlock two helices...

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Metadata

Authors
Hodges, R. S., Sodek, J., Smillie, L. B., & Jurasek, L.
Venue
Cold Spring Harbor Symposia on Quantitative Biology
Published
1973-01-01
Volume
37
Issue
0
Pages
299-310
ISSN
  • 0091-7451 (ISSN-L)
  • 1943-4456
OpenAlex
W2329508872
Cited by
196
References
0
Type
posted content
Language
en
Open access
closed

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CoChat. (2026). Citation check: Tropomyosin: Amino Acid Sequence and Coiled-Coil Structure. https://app.cochat.ai/papers/10.1101/sqb.1973.037.01.040
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Hodges, R. S., Sodek, J., Smillie, L. B., & Jurasek, L. (1973). Tropomyosin: Amino Acid Sequence and Coiled-Coil Structure. Cold Spring Harbor Symposia on Quantitative Biology. https://doi.org/10.1101/sqb.1973.037.01.040

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