In striated muscle, regulation of actin-myosin interactions depends on a series of
conformational changes within the thin filament that result in a shifting of the tropomyosin …

In striated muscle, regulation of actin-myosin interactions depends on a series of
conformational changes within the thin filament that result in a shifting of the tropomyosin …

Striated muscle tropomyosin spans seven actin monomers and contains seven quasi-
repeating regions with loose sequence similarity. Each region contains a hypothesized actin …

Striated muscle thin filaments adopt different quaternary structures, depending upon calcium
binding to troponin and myosin binding to actin. Modification of actin subdomain 2 alters …

The troponin–tropomyosin-linked regulation of striated muscle contraction occurs through
allosteric control by both Ca2+ and myosin. The thin filament fluctuates between two …

About 30 years ago the proceedings of the Cold Spring Harbor Symposium in Quantitative
Biology entitled 'The Mechanism of Muscle Contraction'was published. A key topic in that …

Tropomyosin (TM) is thought to exist in equilibrium between two states on F-actin, closed
and open [Geeves, MA, and Lehrer, SS (1994) Biophys. J. 67, 273− 282]. Myosin shifts the …

The function of three of tropomyosin's sequential quasiequivalent regions was studied by
deletion from skeletal muscle α-tropomyosin of internal residues 49–167. This deletion …

Interactions of the components of reconstituted thin filaments were investigated using a
tropomyosin internal deletion mutant, D234, in which actin-binding pseudo-repeats 2, 3, and …

Tropomyosin (Tm) binds along actin filaments, one molecule spanning four to seven actin
monomers, depending on the isoform. Periodic repeats in the sequence have been …