Range of pH in which unfolding of ordered proteins is common

Range <3 unitless
Organism Budding yeast Saccharomyces cerevisiae
Reference Theillet FX et al., Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chem Rev. 2014 Jul 9 114(13):6661-714. doi: 10.1021/cr400695p p.6665 left column 4th paragraphPubMed ID24901537
Primary Source [100] Fink AL, Calciano LJ, Goto Y, Kurotsu T, Palleros DR. Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry. 1994 Oct 18 33(41):12504-11PubMed ID7918473
Method Primary source [100] abstract: "A systematic investigation of the effect of acid on the denaturation of some 20 monomeric proteins indicates that several different types of conformational behavior occur, depending on the protein, the acid, the presence of salts or denaturant, and the temperature. Three major types of effects were observed. Type I proteins, when titrated with HCl in the absence of salts, show two transitions, initially unfolding in the vicinity of pH 3-4 and then refolding to a molten globule-like conformation, the A state, at lower pH."
Comments P.6665 left column 4th paragraph: "How do changes in intracellular pH affect disordered proteins? Ordered proteins are sensitive to pH, and unfolding is common at pH values <3 (primary source)."
Entered by Uri M
ID 115844