Key result
The kinetic process of the conformational change of TN-C in BIPM-NEM-labeled troponin induced by calcium was biphasic, modified by complex formation with TN-I and TN-T compared to isolated TN-C.
Formation of a complex of TN-C with TN-I and TN-T modifies the molecular kinetic mechanism of the conformational change of TN-C upon calcium binding.
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No immediate clinical implications; leaves open further mechanistic studies on troponin regulation in cardiac contraction.
Iio et al. (1979) studied this question. Calcium binding or removal was evaluated on Kinetics of the conformational change of the troponin-C (TN-C) subunit. The kinetic process of the conformational change of TN-C in BIPM-NEM-labeled troponin induced by calcium was biphasic, modified by complex formation with TN-I and TN-T compared to isolated TN-C.
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