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- W2069864531 abstract "Myocardial contraction is initiated when Ca2+ binds to site II of cardiac troponin C. This 12-residue EF-hand loop (NH2-DEDGSGTVDFDE-COOH) contains six residues (bold) that coordinate Ca2+ binding and six residues that do not appear to influence Ca2+ binding directly. We have introduced six single-cysteine substitutions (italics) within site II of cTnC to investigate whether these residues are essential for Ca2+ binding affinity in isolation and Ca2+ sensitivity of force development in single muscle fibers. Ca2+ binding properties of mutant proteins were examined in solution and after substitution into rat skinned soleus fibers. Except for the serine mutation, cysteine substitution had no effect on Ca2+ binding on cTnC in solution. However, as part of the myofilament, the threonine mutation reduced Ca2+ sensitivity while the phenylalanine mutation increased Ca2+ sensitivity. Analysis of the available crystal and NMR structures reveals specific structural mechanisms for these effects." @default.
- W2069864531 created "2016-06-24" @default.
- W2069864531 creator A5053571370 @default.
- W2069864531 creator A5086476397 @default.
- W2069864531 date "2008-04-15" @default.
- W2069864531 modified "2023-09-27" @default.
- W2069864531 title "Intramolecular Interactions in the N-Domain of Cardiac Troponin C Are Important Determinants of Calcium Sensitivity of Force Development" @default.
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- W2069864531 doi "https://doi.org/10.1021/bi800164c" @default.
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