Work Done by Titin Protein Folding Assists Muscle Contraction

• Published in: Cell reports (Cambridge) Vol. 14; no. 6; pp. 1339 - 1347
• Main Authors: Rivas-Pardo, Jaime Andrés, Eckels, Edward C., Popa, Ionel, Kosuri, Pallav, Linke, Wolfgang A., Fernández, Julio M.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 16.02.2016; Elsevier
• Subjects: Animals; Biomechanical Phenomena; Connectin - chemistry; Connectin - physiology; Elasticity; Humans; Immunoglobulin G - chemistry; Immunoglobulin G - physiology; Mechanotransduction, Cellular; Muscle Contraction - physiology; Muscle, Skeletal - physiology; Muscle, Skeletal - ultrastructure; Myosins - chemistry; Myosins - physiology; Protein Domains; Protein Folding; Rabbits; Sarcomeres - physiology; Sarcomeres - ultrastructure
• ISSN: 2211-1247; 2211-1247
• DOI: 10.1016/j.celrep.2016.01.025

Current theories of muscle contraction propose that the power stroke of a myosin motor is the sole source of mechanical energy driving the sliding filaments of a contracting muscle. These models exclude titin, the largest protein in the human body, which determines the passive elasticity of muscles....