TIMbarrel (triose-phosphate isomerase), also known as an alpha/beta barrel,: 252 is a conserved protein fold consisting of eight alpha helices (α-helices)
parallel to the barrel and the α-helix is in the outside of the barrel but does not contact the α-helices of the other repeats like in TIMbarrels. The protein
therefore mostly parallel. Common examples include the flavodoxin fold, the TIMbarrel and leucine-rich-repeat (LRR) proteins such as ribonuclease inhibitor
all-β, α+β and α/β domains, and in many peptides or small proteins with poorly defined overall architecture. All-β domains may form β-barrels, β-sandwiches
proteins with transmembrane β-barrel and proteins with one or more α-helical membrane anchors. The TOM complex, part of the TOM/TIM supercomplex, is essential