Can the passive elasticity of muscle be explained directly from the mechanics of individual titin molecules?
Recent progress in understanding the role of titin/connectin in muscle elasticity has been heavily based on results from single molecule mechanical experiments. The shape of force-extension curves from such data is similar to curves from muscle fibres and it has been tempting to assume that muscle elasticity can be extrapolated directly from the single molecule data. In this paper we discuss some of the factors that act on titin in the sarcomere that are likely to preclude such a direct extrapolation.
Tskhovrebova
Larissa
L
Astbury Centre for Structural Molecular Biology and School of Biomedical Sciences, University of Leeds, LS2 9JT, Leeds, UKJ.
Houmeida
Ahmed
A
Trinick
John
J
D000818:Animals; D001696:Biomechanical Phenomena; D064211:Connectin; D006801:Humans; D008854:Microscopy, Electron; D008954:Models, Biological; D009119:Muscle Contraction / Q000502:physiology*; D009124:Muscle Proteins / Q000502:physiology*; D009132:Muscles / Q000502:physiology / Q000648:ultrastructure; D011494:Protein Kinases / Q000502:physiology*; D012518:Sarcomeres / Q000502:physiology / Q000648:ultrastructure
D064211:Connectin; D009124:Muscle Proteins; C577285:TTN protein, human; D011494:Protein Kinases