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A transmembrane domain (TMD) is a membrane-spanning protein domain.TMDs may consist of one or several alpha-helices or a transmembrane beta barrel.Because the interior of the lipid bilayer is hydrophobic, the amino acid residues in TMDs are often hydrophobic, although proteins such as membrane pumps and ion channels can contain polar residues.
The database provides information about the individual proteins including computationally generated three-dimensional models of their transmembrane alpha-helices spatially arranged in the membrane, topology, intracellular localizations, amino acid sequences, domain architecture, functional annotation and available experimental structures from ...
The largest and most common human TMEM33 protein is 247 amino acid long protein with 3 transmembrane domains. [11] The only known TMEM33 ortholog with four transmembrane domains is Tts1 in Schizosaccharomyces pombe. [12] The human protein has a predicted molecular weight of 28 kDa [13] and an isoelectric point of 9.88. [14]
In addition to the protein domains, there are unusual transmembrane elements formed by peptides. A typical example is gramicidin A, a peptide that forms a dimeric transmembrane β-helix. [7] This peptide is secreted by gram-positive bacteria as an antibiotic. A transmembrane polyproline-II helix has not been reported in natural proteins ...
Transmembrane protein 145 isoform 1 is rich in phenylalanine and tyrosine. [23] The subcellular localization of the human TMEM145 protein is the plasma membrane and cytoskeleton . [ 8 ] This protein has a signal peptide from amino acid 1-29 and a cleavage site between amino acid 29 and 30. [ 24 ]
Two most abundant classes of transmembrane receptors are GPCR and single-pass transmembrane proteins. [8] [9] In some receptors, such as the nicotinic acetylcholine receptor, the transmembrane domain forms a protein pore through the membrane, or around the ion channel. Upon activation of an extracellular domain by binding of the appropriate ...
A single-pass transmembrane protein typically consists of three domains, the extracellular domain, the transmembrane domain, and the intracellular domain.The transmembrane domain is the smallest at around 25 amino acid residues and forms an alpha helix inserted into the membrane bilayer.
In molecular biology, ATP-binding domain of ABC transporters is a water-soluble domain of transmembrane ABC transporters. ABC transporters belong to the ATP-Binding Cassette superfamily, which uses the hydrolysis of ATP to translocate a variety of compounds across biological membranes. ABC transporters are minimally constituted of two conserved ...