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Titin A-band has homologs in invertebrates, such as twitchin (unc-22) and projectin, which also contain Ig and FNIII repeats and a protein kinase domain. [27] The gene duplication events took place independently but were from the same ancestral Ig and FNIII domains. It is said that the protein titin was the first to diverge out of the family. [25]
In 2011, a dictionary broke this record with a 1909-letter word describing the trpA protein 3] John Horton Conway and Landon Curt Noll developed an open-ended system for naming powers of 10, in which one sexmilliaquingensexagintillion, coming from the Latin name for 6560, is the name for 10 3(6560+1) = 10 19683.
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]
Alpha-actinin-2 is a 103.8 kDa protein composed of 894 amino acids. [6] [7] Each molecule is rod-shaped (35 nm in length) and it homodimerizes in an anti-parallel fashion.. Each monomer has an N-terminal actin-binding region composed of two calponin homology domains, two C-terminal EF hand domains, and four tandem spectrin-like repeats form the rod domain in the central region of the molecule.
The C-terminal end of the titin string extends into the M line, where it binds tightly to Myomesin-1 and myomesin 2. Skelemin/Myomesin-1 is concentrated at peripheral regions of M-bands, and is postulated to link myofibrils with the intermediate filament cytoskeleton. [11] Skelemin/Myomesin-1 has been detected in the nucleus as well as the ...
21393 Ensembl ENSG00000173991 ENSMUSG00000007877 UniProt O15273 O70548 RefSeq (mRNA) NM_003673 NM_011540 RefSeq (protein) NP_003664 NP_003664.1 NP_035670 Location (UCSC) Chr 17: 39.67 – 39.67 Mb Chr 11: 98.27 – 98.28 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Telethonin, also known as Tcap, is a protein that in humans is encoded by the TCAP gene. Telethonin is expressed in ...
Myomesin is bound to myosin at its N-terminal. Obscurin connects the myomesin dimers and binds to the C-terminal of titin. It is thought that the myomesin-titin interaction is vital for the execution of the mechanical functions of the Ser/Thr kinase domain of titin. [2] Myomesin is a protein family found in the M-line of the sarcomere structure.
The I-type Ig-like domains reside at the C-terminal half, and are most homologous to Ig domains 2-3 of palladin and Ig domains 4-5 of myopalladin and more distantly related to Z-disc Ig domains 7 and 8 of titin. The C-terminal region hosts the binding sites for Z-band proteins, and 2 Ig domains are the site of homodimerization for myotilin. [10]