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Titin is the third most abundant protein in muscle (after myosin and actin), and an adult human contains approximately 0.5 kg of titin. [13] With its length of ~27,000 to ~35,000 amino acids (depending on the splice isoform ), titin is the largest known protein . [ 14 ]
Myotilin is a protein that in humans is encoded by the MYOT gene. [ 5 ] [ 6 ] [ 7 ] Myotilin (myofibrillar titin-like protein) also known as TTID (TiTin Immunoglobulin Domain) is a muscle protein that is found within the Z-disc of sarcomeres .
The protein complex composed of actin and myosin, contractile proteins, is sometimes referred to as actomyosin.In striated skeletal and cardiac muscle, the actin and myosin filaments each have a specific and constant length in the order of a few micrometers, far less than the length of the elongated muscle cell (up to several centimeters in some skeletal muscle cells). [5]
The IUPAC name for Titin. This is the largest known protein and so has the longest chemical name. Written in full, it contains 189,819 letters. [48] Periplanone B: Periplanone B A pheromone of the female American cockroach. Thebacon: Thebacon Dihydrocodeinone enol acetate, an opioid analgesic or antitussive. [citation needed]
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.
Telethonin is a 19.0 kDa protein composed of 167 amino acids. [8] Telethonin has a unique β-sheet structure, which enables antiparallel association with the Titin Z1-Z2 domains in cardiac and skeletal muscle. [9]
Schematic representation of structural classes of protein according to the CATH classification scheme. [1] Proteins are a class of macromolecular organic compounds that are essential to life. They consist of a long polypeptide chain that usually adopts a single stable three-dimensional structure.
The number of strands found in such domains may differ from one protein to another. β-sandwich domains are subdivided in a variety of different folds. The immunoglobulin-type fold found in antibodies (Ig-fold) consists of a sandwich arrangement of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek-key topology. [2]