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The Titin protein is located between the myosin thick filament and the Z disk. [22] Titin consists primarily of a linear array of two types of modules, also referred to as protein domains (244 copies in total): type I fibronectin type III domain (132 copies) and type II immunoglobulin domain (112 copies).
Thick filaments consist primarily of the protein myosin, that is responsible for force generation. It is composed of a globular head with both ATP and actin binding sites, and a long tail involved in its polymerization into myosin filaments. Elastic filaments are made up of a giant protein called titin and hold the thick filaments in place.
The IUPAC nomenclature for organic chemical compounds is open-ended, giving rise to the 189,819-letter chemical name Methionylthreonyl threonyl . . . iso leucine for the protein also known as titin, which is involved in striated muscle formation. In nature, DNA molecules can be much bigger than protein molecules and therefore potentially be ...
The main proteins involved are myosin, actin, and titin. Myosin and actin are the contractile proteins and titin is an elastic protein. The myofilaments act together in muscle contraction, and in order of size are a thick one of mostly myosin, a thin one of mostly actin, and a very thin one of mostly titin. [1] [2]
The giant protein titin (connectin) extends from the Z-line of the sarcomere, where it binds to the thick filament (myosin) system, to the M-band, where it is thought to interact with the thick filaments. Titin (and its splice isoforms) is the biggest single highly elasticated protein found in nature.
Even the smallest proteins contain no fewer than 20 amino acids, making for some pretty long names in their own right; titin, however, is the human body’s largest protein. Total amino acid count ...
Obscurin is a protein that in humans is encoded by the OBSCN gene. [5] [6] [7] Obscurin belongs to the family of giant sarcomeric signaling proteins that includes titin and nebulin. Obscurin is expressed in cardiac and skeletal muscle, and plays a role in the organization of myofibrils during sarcomere assembly.
The giant protein titin, together with its associated proteins, interconnects the major structure of sarcomeres, the M bands and Z discs. The C-terminal end of the titin string extends into the M line , where it binds tightly to M-band constituents MYOM1 and M-protein, of apparent molecular masses of 190 kD and 165 kD, respectively.