Reversible folding energetics of Yersinia Ail barrel reveals a hyperfluorescent intermediate.

ABSTRACT: Deducing the molecular details of membrane protein folding has lately become an important area of research in biology. Using Ail, an outer membrane protein (OMP) from Yersina pestis as our model, we explore details of β-barrel folding, stability, and unfolding. Ail displays a simple transmembrane β-barrel topology. Here, we find that Ail follows a simple two-state mechanism in its folding and unfolding thermodynamics. Interestingly, Ail displays multi-step folding kinetics. The early kinetic intermediates in the folding pathway populate near the unfolded state (β_T ≈ 0.20), and do not display detectable changes in the local environment of the two interface indoles. Interestingly, tryptophans regulate the late events of barrel rearrangement, and Ail thermodynamic stability. We sho

SUBMITTER: Gupta A 

PROVIDER: S-EPMC7612366 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature