Key result
Hydrophobic residue substitutions to polar Gln in the N-domain of cardiac troponin C(F27W) increased calcium affinity by 2.1-15.2-fold, primarily due to faster calcium association rates.
Population
Human cardiac troponin C (in vitro model)
Comparison
Substitution of hydrophobic residues with polar… vs Unmutated cardiac troponin C(F27W)
Design
Preclinical
Authors
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May guide troponin C engineering for calcium sensitization; leaves open in vivo cardiac effects and therapeutic translation.
Effect estimate: 2.1-15.2-fold increase
Specific polar substitutions in the N-domain of cardiac troponin C increase calcium affinity primarily by accelerating calcium association, offering insights into the structural regulation of cardiac muscle contraction.
Tikunova et al. (2004) studied this question. Hydrophobic residue substitutions (Phe20, Val44, Met45, Leu48, Met81 to Gln) in cardiac troponin C(F27W) vs. Unmutated cardiac troponin C(F27W) was evaluated on Calcium affinity of the regulatory domain (2.1-15.2-fold increase). Hydrophobic residue substitutions to polar Gln in the N-domain of cardiac troponin C(F27W) increased calcium affinity by 2.1-15.2-fold, primarily due to faster calcium association rates.
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