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all-beta folds in SCOP database (folds 54 to 100 are water-soluble beta-barrels). CATH database - folds and homologous superfamilies within the beta-barrel architecture. General classification and images of protein structures from Jane Richardson lab; Images and examples of transmembrane beta-barrels
All beta-barrel transmembrane proteins have simplest up-and-down topology, which may reflect their common evolutionary origin and similar folding mechanism. [7] 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 ...
Porins are beta barrel proteins that cross a cellular membrane and act as a pore, through which molecules can diffuse. [1] Unlike other membrane transport proteins, porins are large enough to allow passive diffusion, i.e., they act as channels that are specific to different types of molecules.
A transmembrane domain (TMD, TM domain) 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.
Beta barrel proteins, which are found only in outer membranes of Gram-negative bacteria, and outer membranes of mitochondria and chloroplasts. [6] Bitopic proteins are transmembrane proteins that span across the membrane only once. Transmembrane helices from these proteins have significantly different amino acid distributions to transmembrane ...
The outer membrane mitochondrial proteins carry out functions for mitochondrial biogenesis and integration between mitochondria and the cellular system. The outer membrane consists of two types of integral proteins, including proteins with transmembrane β-barrel and proteins with one or more α-helical membrane anchors. [5] [6]
Topology of a transmembrane protein refers to locations of N- and C-termini of membrane-spanning polypeptide chain with respect to the inner or outer sides of the biological membrane occupied by the protein. [1] Group I and II transmembrane proteins have opposite final topologies. Group I proteins have the N terminus on the far side and C ...
Mycobacterial porins are a group of transmembrane beta-barrel proteins produced by mycobacteria, which allow hydrophilic nutrients to enter the bacterium. [1] [2] They are located in the impermeable mycobacterial outer membrane, or mycomembrane of fast-growing mycobacteria. The mycomembrane is unique and composed of very-long chain fatty acids ...