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• W4243512353 abstract "Abstract Protein design advancements have led to biotechnological strategies based on more stable and more specific structures. Herein we present a 6‐residue sequence (HPATGK) that acts as a stable structure‐nucleating turn at physiological and higher pH but is notably unfavorable for chain direction reversal at low pH. When placed into the turn of a β‐sheet, this leads to a pH switch of folding. Using a standard 3‐stranded β‐sheet model, the WW domain, it was found that the pH switch sequence insertion caused minimal change at pH 8 but a ca. 50 °C drop in the melting temperature (T m ) was observed at pH 2.5: ΔΔG F ≥11.3 kJ mol −1 . Using the strategies demonstrated in this article, the redesign of β‐sheets to contain a global, or local, pH‐dependent conformational switch should be possible." @default.
• W4243512353 created "2022-05-12" @default.
• W4243512353 creator A5031107434 @default.
• W4243512353 creator A5039508071 @default.
• W4243512353 date "2017-05-19" @default.
• W4243512353 modified "2023-10-16" @default.
• W4243512353 title "A pH Switch for β-Sheet Protein Folding" @default.
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• W4243512353 doi "https://doi.org/10.1002/ange.201700860" @default.
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