Key result
The N-extension of cardiac troponin I is primarily disordered but forms specific stable extended and alpha-helical structures at phosphorylation sites when complexed with troponin C at low ionic strength.
Population
Cardiac troponin I (cTnI) and troponin C (cTnC) complexes
Comparison
Monomeric state vs cTnI-cTnC complex at 0.1 M KCl vs 0.2 M KCl
Design
In vitro biophysical study using site-directed spin labeling electron paramagnetic resonance
Authors
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No direct clinical translation; hypothesis-generating for troponin dynamics in animal models.
The N-extension of cardiac troponin I exhibits dynamic structural changes and interacts stereospecifically with troponin C at phosphorylation regions, which is modulated by ionic strength.
Zhao et al. (2019) studied this question. Complex formation with cTnC at varying ionic strengths vs. Monomeric cTnI was evaluated on Interresidual distance distribution between spin labels attached to i and i+4 residues. The N-extension of cardiac troponin I is primarily disordered but forms specific stable extended and alpha-helical structures at phosphorylation sites when complexed with troponin C at low ionic strength.
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