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Article

Tropomyosin Must Interact Weakly with Actin to Effectively Regulate Thin Filament Function.

Biophysical journal - 5 Dec 2017

Rynkiewicz Michael J, Prum Thavanareth, Hollenberg Stephen, Kiani Farooq A, Fagnant Patricia M, Marston Steven B, Trybus Kathleen M, Fischer Stefan, Moore Jeffrey R, Lehman William

Abstract excerpt

Elongated tropomyosin, associated with actin-subunits along the surface of thin filaments, makes electrostatic interactions with clusters of conserved residues, K326, K328, and R147, on actin. The association is weak, permitting low-energy cost regulatory movement of tropomyosin across the filament during muscle activation. Interestingly, acidic D292 on actin, also evolutionarily conserved, lies adjacent to the...

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Identifiers

PMID: 29211998
DOI: 10.1016/j.bpj.2017.10.004
PMCID: PMC5768522

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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