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Inhibition of mutant troponin C activity by an intra-domain disulphide bond

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Abstract

Triggering of contraction in striated muscles involves a conformational transition in the N-terminal domain of troponin C, the calcium-binding component of thin filaments. We have designed a mutant troponin C in which the key conformational transition and the calcium-regulatory activity are reversibly blocked by the formation of a disulphide bridge. Our results may be applicable to other proteins of the same family of calcium-binding proteins.

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Grabarek, Z., Tan, RY., Wang, J. et al. Inhibition of mutant troponin C activity by an intra-domain disulphide bond. Nature 345, 132–135 (1990). https://doi.org/10.1038/345132a0

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