JA. Herzog∗, TR. Leonard†, A. Jinha†, W. Herzog†,‡
Molecular & Cellular Biomechanics, Vol.11, No.1, pp. 1-17, 2014, DOI:10.3970/mcb.2014.011.001
Abstract Titin is the third most abundant protein in sarcomeres and fulfills a number of mechanical and signaling functions. Specifically, titin is responsible for most of the passive forces in sarcomeres and the passive visco-elastic behaviour of myofibrils and muscles. It has been suggested, based on mechanical testing of isolated titin molecules, that titin is an essentially elastic spring if Ig domain un/refolding is prevented either by working at short titin lengths, prior to any unfolding of Ig domains, or at long sarcomere (and titin) lengths when Ig domain un/refolding is effectively prevented. However, these properties of titin, and by extension… More >
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