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Linje 155: == BETA BARREL == https://en.wikipedia.org/wiki/Beta_barrel Beta-barrel proteins are ~~so far~~ found ~~only~~ in outer membranes of [[gram-negative bacteria]], [[cell wall]] of [[gram-positive bacteria]], and [[Outer mitochondrial membrane\|outer membranes]] of [[mitochondria]] and [[chloroplasts]]. All beta-barrel transmembrane proteins have simplest up-and-down topology, which may reflect their common evolutionary origin and similar folding mechanism. I mitochondrier og chloroplastre http://rspb.royalsocietypublishing.org/content/273/1596/1943 * SAM50 https://en.wikipedia.org/wiki/Sorting_and_assembly_machinery * TOM40 https://en.wikipedia.org/wiki/Translocase_of_the_outer_membrane ~~Også~~* lipocaliner * Retinolbindende protein https://en.wikipedia.org/wiki/Retinol_binding_protein * Major urinary proteins, 0 i mennesker til mindst 21i mus https://en.wikipedia.org/wiki/Major_urinary_proteins * Poriner https://en.wikipedia.org/wiki/Porin_(protein) https://da.wikipedia.org/wiki/Poriner ~~Eight-stranded beta barrel.[1]~~ ~~OmpA og OmpA-like TMD.~~ OmpA is the predominant cell surface antigen in enterobacteria found in about 100,000 copies per cell▼ ▲* OmpA og OmpA-like TMD. Eight-stranded beta barrel.[1] OmpA is the predominant cell surface antigen in enterobacteria found in about 100,000 copies per cell * C9, MAC https://royalsocietypublishing.org/doi/10.1098/rstb.2016.0221#RSTB20160221C45R▼ * C9, MAC Membrane attack complex/perforin-like (MACPF) proteins comprise the largest superfamily of pore-forming proteins, playing crucial roles in immunity and pathogenesis. Soluble monomers assemble into large transmembrane pores via conformational transitions. the membrane attack complex/perforin (MACPF) domain, and revealed an evolutionary link to the cholesterol-dependent cytolysin (CDC) family of bacterial toxins despite limited sequence identity [40,41]. As such, proteins across a wide range of genera and species that share this fold are often referred to as belonging to the MACPF/CDC superfamily [42]. The MACPF/CDC fold is composed of approximately 350 amino acids and includes a central antiparallel, twisted β-sheet. The central β-sheet is bent nearly 90° and is flanked by two clusters of α-helices. During conversion to the pore, both clusters unfurl to form two antiparallel transmembrane β-hairpins (TMHs) that comprise the final β-barrel [43–45] (figure 2f). ▲* C9, MAC https://royalsocietypublishing.org/doi/10.1098/rstb.2016.0221#RSTB20160221C45R https://scholar.google.com/scholar_lookup?hl=en&volume=10&publication_year=2008&pages=1765-1774&journal=Cell.+Microbiol.&author=CJ+Rosado&title=The+MACPF%2FCDC+family+of+pore-forming+toxins * Clostridium perfringens perfringolysin O (PFO or θ-toxin) is a cytolytic toxin that binds to cholesterol-containing membranes and then self-associates to spontaneously form aqueous pores of varying size in the bilayer. https://scholar.google.com/scholar_lookup?hl=en&volume=37&publication_year=1998&pages=14+563-14+574&journal=Biochemistry&author=LA+Shepard&author=AP+Heuck&author=BD+Hamman&author=J+Rossjohn&author=MW+Parker&author=KR+Ryan&author=AE+Johnson&author=RK+Tweten&title=Identification+of+a+membrane-spanning+domain+of+the+thiol-activated+pore-forming+toxin+Clostridium+perfringens+perfringolysin+O%3A+an+α-helical+to+β-sheet+transition+identified+by+fluorescence+spectroscopy * Pleurotolysin https://scholar.google.com/scholar_lookup?hl=en&volume=13&publication_year=2015&pages=1-15&journal=PLoS+Biol.&author=N+Lukoyanova&title=Conformational+changes+during+pore+formation+by+the+perforin-related+protein+pleurotolysin * søg pore forming toxin == MANGE TMD ==

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