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Microtubule and tubulin metrics [1]. Microtubules are polymers of tubulin that form part of the cytoskeleton and provide structure and shape to eukaryotic cells. Microtubules can be as long as 50 micrometres, as wide as 23 to 27 nm [2] and have an inner diameter between 11 and 15 nm. [3]
Tubulin in molecular biology can refer either to the tubulin protein superfamily of globular proteins, or one of the member proteins of that superfamily. α- and β-tubulins polymerize into microtubules, a major component of the eukaryotic cytoskeleton. [1]
In cell biology, microtubule nucleation is the event that initiates de novo formation of microtubules (MTs). These filaments of the cytoskeleton typically form through polymerization of α- and β-tubulin dimers, the basic building blocks of the microtubule, which initially interact to nucleate a seed from which the filament elongates.
Tubulin alpha-1A chain is a protein that in humans is encoded by the TUBA1A gene. [ 5 ] [ 6 ] [ 7 ] Tubulin alpha-1A chain is a type of alpha-tubulin involved in the formation of microtubules , which are structural proteins that play a role in the cytoskeletal structure.
MAPs bind to the tubulin subunits that make up microtubules to regulate their stability. A large variety of MAPs have been identified in many different cell types, and they have been found to carry out a wide range of functions. These include both stabilizing and destabilizing microtubules, guiding microtubules towards specific cellular ...
γ-tubulin is a protein located at the centrosome that nucleates the microtubules by interacting with the tubulin monomer subunit in the microtubule at the minus end. [1] Organization of the microtubules at the MTOC, or centrosome in this case, is determined by the polarity of the microtubules defined by y-tubulin. [1]
A mitotic inhibitor, microtubule inhibitor, or tubulin inhibitor, is a drug that inhibits mitosis, or cell division, and is used in treating cancer, gout, and nail fungus. These drugs disrupt microtubules, which are structures that pull the chromosomes apart when a cell divides.
The tubulin protein dimers of the microtubules have hydrophobic pockets that may contain delocalized π electrons. Tubulin has other, smaller non-polar regions, for example 8 tryptophans per tubulin, which contain π electron-rich indole rings distributed throughout tubulin with separations of roughly 2 nm.