Jump to Main Content
- Czajkowska, Marta, et al. Show all 8 Authors
- TheFEBS journal 2019 v.286 no.10 pp. 1877-1893
- actin; adenosinetriphosphatase; calcium; energy; enzyme activity; enzyme inhibition; genes; microfilaments; molecular dynamics; muscle contraction; muscle fibers; muscular diseases; mutation; myosin; polymerization; simulation models; tropomyosins; van der Waals forces
- ... Tropomyosin (Tpm) binds along actin filaments and regulates myosin binding to control muscle contraction. Tropomodulin binds to the pointed end of a filament and regulates actin dynamics, which maintains the length of a thin filament. To define the structural determinants of these Tpm functions, we examined the effects of two congenital myopathy mutations, A4V and R91C, in the Tpm gene, TPM3, whic ...
- Czajkowska, Marta, et al. Show all 5 Authors
- Biochimica et biophysica acta 2018 v.1866 pp. 558-568
- actin; calcium; cardiomyopathy; enzyme activity; microfilaments; muscle contraction; mutants; mutation; myosin; phenotype; polymerization; tropomyosins
- ... Tropomyosin polymerizes along actin filaments and together with troponin regulates muscle contraction in a Ca-dependent manner. Actin-binding periods are homologous residues, which repeat along tropomyosin sequence, form tropomyosin-actin interface and determine regulatory functions. To learn how period 3 is involved in tropomyosin functions we examined effects of two mutations in Tpm1.1, I92T and ...