Key result
In the presence of calcium, the titin I27 homopolymer chain became stabilized, requiring higher stretching forces to unfold, with increased stiffness and peak-to-peak distance between domains.
Population
Titin immunoglobulin domain 27 (I27) homopolymer chain
Comparison
Calcium exposure during stretching vs Stretching in the absence of calcium (implied)
Design
Preclinical
Authors
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May influence passive muscle force; leaves open titin-calcium effects on diastolic properties pending in vivo studies.
Calcium interacts with titin immunoglobulin domain 27 to stabilize it, increasing its resistance to stretch and modulating passive force in muscle.
DuVall et al. (2012) studied this question. Calcium vs. Absence of calcium was evaluated on Mechanical properties of titin I27 domain (unfolding force, stiffness, peak-to-peak distance). In the presence of calcium, the titin I27 homopolymer chain became stabilized, requiring higher stretching forces to unfold, with increased stiffness and peak-to-peak distance between domains.
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