Lipid bilayer induces contraction of the denatured state ensemble of a helical-bundle membrane protein.

ABSTRACT: Defining the denatured state ensemble (DSE) and disordered proteins is essential to understanding folding, chaperone action, degradation, and translocation. As compared with water-soluble proteins, the DSE of membrane proteins is much less characterized. Here, we measure the DSE of the helical membrane protein GlpG of Escherichia coli (E. coli) in native-like lipid bilayers. The DSE was obtained using our steric trapping method, which couples denaturation of doubly biotinylated GlpG to binding of two streptavidin molecules. The helices and loops are probed using limited proteolysis and mass spectrometry, while the dimensions are determined using our paramagnetic biotin derivative and double electron-electron resonance spectroscopy. These data, along with our Upside sim

SUBMITTER: Gaffney KA 

PROVIDER: S-EPMC8740594 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature