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Beta barrels also function within endosymbiont derived organelles such as mitochondria and chloroplasts to transport proteins. [8] Within the mitochondrion two complexes exist with beta barrels serving as the pore forming subunit, Tom40 of the Translocase of the outer membrane, and Sam50 of the Sorting and assembly machinery. The chloroplast ...
There are two basic types of transmembrane proteins: [4] alpha-helical and beta barrels. Alpha-helical proteins are present in the inner membranes of bacterial cells or the plasma membrane of eukaryotic cells, and sometimes in the bacterial outer membrane. [5] This is the major category of transmembrane proteins.
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.
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 ...
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.
OmpA-like transmembrane domain is an evolutionarily conserved domain of bacterial outer membrane proteins. This domain consists of an eight-stranded beta barrel. [1] OmpA is the predominant cell surface antigen in enterobacteria found in about 100,000 copies per cell. [2] The expression of OmpA is tightly regulated by a variety of mechanisms.
Although maltoporin contains a wider beta-barrel than the porins of the GBP and RPP families, it exhibits a narrower channel, showing only 5% of the ionic conductance of the latter porins. The Rhodobacter PorCa Protein, the only well characterized member of the RPP family, was the first porin to yield its three-dimensional structure by X-ray ...
BamA is a β-barrel, outer membrane protein found in Gram-negative bacteria and it is the main and vital component of the β-barrel assembly machinery (BAM) complex in those bacteria. [1] BAM Complex consists of five components; BamB, BamC, BamD, BamE (all are lipoproteins ) and BamA (Outer membrane protein).