Clusters of bound Ca(2+) initiate contraction in fast skeletal muscle.

Ca(2+)-binding to troponin C ultimately controls force in muscle leading to the expectation that the two curves, pCa/force and pCa/Ca(2+) binding, will coincide. Using an improved fluorescence apparatus to measure Ca(2+)-binding, we confirm a displacement between the position and shape of the pCa/Ca(2+)-binding and pCa/force curves. This displacement may be part of a mechanism that reduces the noise inherent in the control process.

The troponin I: inhibitory peptide uncouples force generation and the cooperativity of contractile activation in mammalian skeletal muscle.

Hodges and his colleagues identified a 12 amino acid fragment of troponin I (TnI-ip) that inhibits Ca(2+)-activated force and reduces the effectiveness Ca(2+) as an activator. To understand the role of troponin C (TnC) in the extended cooperative interactions of thin filament activation, we compared the effect of TnI-ip with that of partial troponin TnC extraction. Both methods reduce maximal Ca(2+)-activated force and increase [Ca(2+)] required for activation.