Extensibility in the titin molecule and its relation to muscle elasticity.
Studies of the origins of muscle passive tension have revealed a direct relationship between elasticity and the mechanical properties of the titin molecule. 'Molecular combing' has made it possible to visualize with high resolution changes in the configuration and structure of isolated titin caused by mechanical forces. The differential extensibility seen in individual molecules is consistent with the important role suggested for the PEVK-region in muscle elasticity. An additional factor emphasizing compliance of this part of the molecule in muscle may relate to the arrangement of the titin filament system in the sarcomere, in particular to titin interactions with thick and thin filaments. The branching of titin network near the PEVK-region suggests that, in addition to conferring extensibility, it may also be important in facilitating the transition of titin intermolecular interactions between the arrays of thick and thin filaments.
Tskhovrebova
L
L
School of Biomedical Sciences, University of Leeds, UK.
Trinick
J
J
D000595:Amino Acid Sequence; D000818:Animals; D064211:Connectin; D004548:Elasticity; D008854:Microscopy, Electron; D009124:Muscle Proteins / Q000737:chemistry* / Q000502:physiology / Q000648:ultrastructure*; D018482:Muscle, Skeletal / Q000502:physiology*; D009210:Myofibrils / Q000502:physiology / Q000648:ultrastructure; D011487:Protein Conformation; D011489:Protein Denaturation; D011494:Protein Kinases / Q000737:chemistry* / Q000502:physiology / Q000648:ultrastructure*; D011817:Rabbits; D012518:Sarcomeres / Q000502:physiology / Q000648:ultrastructure*
D064211:Connectin; D009124:Muscle Proteins; D011494:Protein Kinases