How to Tailor Giant Proteoliposomes

Fenz, Susanne F.; Sachse, Rita; Kubick, Stefan; Schmidt, Thomas

doi:10.1016/j.bpj.2011.11.121

Cited by 1 publication

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“…Cell-free expression (also known as in vitro transcription/ translation, IVTT) of membrane proteins has been used for a number of years as a method for the expression of toxic and difficult-to-express proteins [86]. Cell-free expression often uses a cell lysate, which contains the cell transcription/ translation machinery and can be derived from E. coli (known as an S30 extract), yeast, wheat germ and rabbit reticulocytes [12,[87][88][89][90][91][92][93][94][95][96][97][98]. Alternatively a cell-free system composed of recombinantly expressed and purified transcription/translation components (e.g.…”

Section: Co-translational Cell-free Methodsmentioning

confidence: 99%

Methods to study folding of alpha-helical membrane proteins in lipids

et al. 2022

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How alpha-helical membrane proteins fold correctly in the highly hydrophobic membrane interior is not well understood. Their folding is known to be highly influenced by the lipids within the surrounding bilayer, but the majority of folding studies have focused on detergent-solubilized protein rather than protein in a lipid environment. There are different ways to study folding in lipid bilayers, and each method has its own advantages and disadvantages. This review will discuss folding methods which can be used to study alpha-helical membrane proteins in bicelles, liposomes, nanodiscs or native membranes. These folding methods include in vitro folding methods in liposomes such as denaturant unfolding studies, and single-molecule force spectroscopy studies in bicelles, liposomes and native membranes. This review will also discuss recent advances in co-translational folding studies, which use cell-free expression with liposomes or nanodiscs or are performed in vivo with native membranes.

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