@Article{mcb.2014.011.001,
AUTHOR = {JA.  Herzog, TR.  Leonard, A.  Jinha, W. Herzog},
TITLE = {Titin (Visco-) Elasticity in Skeletal Muscle Myofibrils},
JOURNAL = {Molecular \& Cellular Biomechanics},
VOLUME = {11},
YEAR = {2014},
NUMBER = {1},
PAGES = {1--17},
URL = {http://www.techscience.com/mcb/v11n1/28560},
ISSN = {1556-5300},
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 of muscles, have not been tested with titin in its natural structural environment within a sarcomere. The purpose of this study was to gain insight into the Ig domain un/refolding kinetics and test the idea that titin could behave essentially elastically at any sarcomere length by preventing Ig domain un/refolding during passive stretch-shortening cycles. Although not completely successful, we demonstrate here that titin’s visco-elastic properties appear to depend on the Ig domain un/refolding kinetics and that indeed, titin (and thus myofibrils) can become virtually elastic when Ig domain un/refolding is prevented.},
DOI = {10.3970/mcb.2014.011.001}
}