Key result
Mutations in the first half of periods 2, 4, and 5 of rat striated muscle αTm resulted in a >4-fold reduction in actin affinity, identifying these as key actin-binding sites.
Population
70 coding sequences of Tm genes from 26 animal species; rat striated muscle αTm expressed in Escherichia coli
Design
Preclinical
Authors
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May guide thin-filament research in cardiomyopathy models; leaves open translation to human disease.
Effect estimate: > 4-fold reduction
Molecular evolution analysis combined with mutagenesis identified specific evolutionarily conserved surface residues in tropomyosin that are critical for actin binding.
Barua et al. (2011) studied this question. Mutations in conserved surface residues of rat striated muscle αTm was evaluated on Actin affinity and thermodynamic stability (> 4-fold reduction). Mutations in the first half of periods 2, 4, and 5 of rat striated muscle αTm resulted in a >4-fold reduction in actin affinity, identifying these as key actin-binding sites.
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