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Role of Titin in Vertebrate Striated Muscle
L. Tskhovrebova and J. Trinick
Philosophical Transactions: Biological Sciences
Vol. 357, No. 1418, Elastomeric Proteins: Structures, Biomechanical Properties and Biological Roles (Feb. 28, 2002), pp. 199-206
Published by: Royal Society
Stable URL: http://www.jstor.org/stable/3066853
Page Count: 8
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Titin is a giant muscle protein with a molecular weight in the megaDalton range and a contour length of more than 1 mm. Its size and location within the sarcomere structure determine its important role in the mechanism of muscle elasticity. According to the current consensus, elasticity stems directly from more than one type of spring-like behaviour of the I-band portion of the molecule. Starting from slack length, extension of the sarcomere first causes straightening of the molecule. Further extension then induces local unfolding of a unique sequence, the PEVK region, which is named due to the preponderance of these amino-acid residues. High speeds of extension and/or high forces are likely to lead to unfolding of the β-sandwich domains from which the molecule is mainly constructed. A release of tension leads to refolding and recoiling of the polypeptide. Here, we review the literature and present new experimental material related to the role of titin in muscle elasticity. In particular, we analyse the possible influence of the arrangement and environment of titin within the sarcomere structure on its extensible behaviour. We suggest that, due to the limited conformational space, elongation and compression of the molecule within the sarcomere occur in a more ordered way or with higher viscosity and higher forces than are observed in solution studies of the isolated protein.
Philosophical Transactions: Biological Sciences © 2002 Royal Society