Search results
Results from the WOW.Com Content Network
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 ]
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]
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]
58916 Ensembl ENSG00000120729 ENSMUSG00000024471 UniProt Q9UBF9 Q9JIF9 RefSeq (mRNA) NM_006790 NM_001135940 NM_001300911 NM_001033621 RefSeq (protein) NP_001129412 NP_001287840 NP_006781 NP_001028793 Location (UCSC) Chr 5: 137.87 – 137.89 Mb Chr 18: 44.47 – 44.49 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Myotilin is a protein that in humans is encoded by the MYOT gene ...
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.
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.
Similar to titin, it is thought to act as a molecular ruler along for thin filament assembly. Several proteins important for the stability of the sarcomeric structure are found in the Z-line as well as in the M-band of the sarcomere. Actin filaments and titin molecules are cross-linked in the Z-disc via the Z-line protein alpha-actinin.
Nebulin is another protein that can bind to the sides of the actin preventing the attachment of myosin to them. This causes stabilization of the actin limiting muscle contraction. Titin is another protein, but it binds to the myosin rather than the actin microfilament. Titin will help stabilize the contraction and myosin-actin structure.