Beta barrel
![A canonical beta-barrel protein, a sucrose-specific porin from the bacterium Salmonella typhimurium, viewed from the side. Porins are transmembrane proteins with hollow centers through which small molecules can diffuse.](/Images/godic/202412/24/Sucrose_porin_1a0s0635.png")
![The human retinol-binding protein (RBP), a canonical lipocalin eight-strand barrel binding retinol (vitamin A).](/Images/godic/202412/24/Rbp_1brp0635.png")
![A mouse major urinary protein bound to 2-sec-butyl-4,5-dihydrothiazole (SBT), a mouse pheromone.[6] The beta barrel forms a calyx, in which the SBT molecule is tightly bound.](/Images/godic/202412/24/MupwithSBT0635.jpg")
![](/Images/godic/202412/24/1RRX_pdb_structures0635.png")
A beta barrel is a large beta-sheet that twists and coils to form a closed structure in which the first strand is hydrogen bonded to the last. Beta-strands in beta-barrels are typically arranged in an antiparallel fashion. Barrel structures are commonly found in porins and other proteins that span cell membranes and in proteins that bind hydrophobic ligands in the barrel center, as in lipocalins. Porin-like barrel structures are encoded by as many as 2–3% of the genes in Gram-negative bacteria.