Cox, Dezerae published the artcileHidden information on protein function in censuses of proteome foldedness, Safety of (S)-2-Amino-4-(methylthio)butanoic acid, the publication is Nature Communications (2022), 13(1), 1992, database is CAplus and MEDLINE.
Methods that assay protein foldedness with proteomics have generated censuses of apparent protein folding stabilities in biol. milieu. However, different censuses poorly correlate with each other. Here, we show that the reason for this is that methods targeting foldedness through monitoring amino acid sidechain reactivity also detect changes in conformation and ligand binding, which can be a substantial fraction of the data. We show that the reactivity of only one quarter of cysteine or methionine sidechains in proteins in a urea denaturation curve of mammalian cell lysate can be confidently explained by a two-state unfolding isotherm. Contrary to that expected from unfolding, up to one third of the cysteines decreased reactivity. These cysteines were enriched in proteins with functions relating to unfolded protein stress. One protein, chaperone HSPA8, displayed changes arising from ligand and cofactor binding. Unmasking this hidden information using the approaches outlined here should improve efforts to understand both folding and the remodeling of protein function directly in complex biol. settings.
Nature Communications published new progress about 63-68-3. 63-68-3 belongs to catalysis-chemistry, auxiliary class Natural product, name is (S)-2-Amino-4-(methylthio)butanoic acid, and the molecular formula is C5H11NO2S, Safety of (S)-2-Amino-4-(methylthio)butanoic acid.
Referemce:
https://courses.lumenlearning.com/boundless-chemistry/chapter/catalysis/,
Catalysis – Wikipedia