titin

The longest technical word in English is the scientific name for the protein titin, at 189,819 letters.

Studies have shed light on a large protein within skeletal muscles named titin.

Of the many titin variants identified, five are described with complete transcript information available.

Among the known structures, titin has a D E modification.

Similar to Titin, it is thought to act as a molecular ruler along for thin filament assembly.

Autoantibodies to titin are produced in patients with the autoimmune disease scleroderma.

The human gene that encodes titin is found on chromosome 2 and contains 363 exons.

Full chemical name of titin.

The following table lists the known titin isoforms:

The name titin is derived from the Greek Titan (a giant deity, anything of great size).

Elastic filaments, 1 nm in diameter, are made of titin, a large springy protein.

Furthermore the gene for titin contains the largest number of exons (363) discovered in any single gene.

Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases.

His other successes included "Titin" to a libretto by Gaston Dumestre.

Proteins can be very short peptide like Enkephalin, or very long like Titin.

Thick filaments consist primarily of the protein myosin, held in place by titin filaments.

A number of titin isoforms are produced in different striated muscle tissues as a result of alternative splicing.

As the largest known protein, titin also has the longest IUPAC name.

Myofibrils are composed of long proteins such as actin, myosin, and titin, and other proteins that hold them together.

Considerable variability exists in the I-band, the M-line and the Z-disc regions of titin.

The giant 30,000 residue muscle protein titin comprises about 120 fibronectin-III-type and Ig-type domains.

Actin filaments and titin molecules are cross-linked in the Z-disc via the Z-line protein alpha-Actinin.

However the actions of elastic proteins such as Titin are hypothesised to maintain uniform tension across the sarcomere and pull the thick filament into a central position.

This sustained phase or catch phase has been attributed to a catch protein that is similar to myosin light-chain kinase and titin, called twitchin.

In mature sarcomeres, wild-type myotilin co-localises with alpha-actinin and Z-disc titin, showing the striated pattern typical of sarcomeric proteins.