Folding TolC in vitro is concentration dependent

It’s tricky to refold membrane proteins! One particular challenge is to refold multi-chain β-barrels. So, often they have to be purified from native membranes. Our lab has a new paper out on folding the multi-chain β-barrel TolC which is the outer membrane part of an antibiotic resistance pump. Jimmy Budiardjo and Ayotunde Paul Ikujuni found that the trick to folding it was to concentrate it in the presence of a membrane mimetic. Undergraduate Andres Cordova saw that folding it this way in vitro maintained native function. Then Emre Firlar and Jason Kaelber showed that folding it this way in vitro had 2D class averages consistent with the native fold. The article is part of an Festschrift celebrating Steve White’s 80th birthday and his amazing contributions to understanding membrane protein folding.

Happy birthday, Steve!