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

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...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Julkaisussa:Biophys J
Päätekijät: 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
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: The Biophysical Society 2017
Aiheet:
Molecular Machines, Motors, and Nanoscale Biophysics
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC5768522/
https://ncbi.nlm.nih.gov/pubmed/29211998
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2017.10.004
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