In molecular biology, autotransporter proteins are proteins secreted out the Gram-negative bacteria. These beta helixes require a domain which is called the intramolecular<unk>  domain. It shows similarities with other intramolecular chaperone sequences and has a folding-associated function. This increases the efficiency, either by stabilizing the beta-barrel, or by promoting the folding of the passenger domain. The<unk>  domain is usually located between the HSF and the passenger domain. When the passenger domain is translocated, starting with its C terminus, the<unk>  domain is first out. This would result in the formation of a hairpin structure.
Autochaperone
Bryostatin
Prohormone
Haptocorrin
Tetanospasmin
Endrin
Clastogen
Coricidin