ArticleBiochimica et biophysica acta. Biomembranes2020
Reversible folding energetics of Yersinia Ail barrel reveals a hyperfluorescent intermediate.
Article in Biochimica et biophysica acta. Biomembranes, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Engineering a HyperstableJournal of the American Chemical Society · 2022Article
- Single-residue physicochemical characteristics kinetically partition membrane protein self-assembly and aggregation.The Journal of biological chemistry · 2020Article
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2 authors.
Funding
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
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