Fig. 2: Concentrated LiBr solutions induce universal protein conformational change and cause denaturation. | Nature Communications

Fig. 2: Concentrated LiBr solutions induce universal protein conformational change and cause denaturation.

From: Entropy-driven denaturation enables sustainable protein regeneration through rapid gel-solid transition

Fig. 2

a Schematics of DHFR, fibronectin, and α-keratin (wool), representing three levels of structural complexity. b–d Turbidity assay of three respective proteins measured by OD405, suggesting different denaturation capabilities of LiBr, LiCl, and NaBr. Data are normalized by the highest OD405 values of respective proteins and presented as mean (n = 4 independently prepared protein solutions). e–g FTIR of the amide I band indicate a gradual loss of secondary structure upon increasing of LiBr concentration. h Percentage change of the secondary structure in DHFR in 2 M LiBr, deconvoluted from the amide I band of Raman spectra. i DLS measurement of the hydrodynamic radius of fibronectin with increasing LiBr concentration, indicating an extension of quaternary structure followed by aggregation. Box plots represent the interquartile range (25th to 75th percentile), with the center line indicating the median. Whiskers extend to the minimum and maximum values. (n = 6 independently prepared protein solutions). j SEM image of wool prior (i) and after (ii) denaturation with 8 M LiBr. Scale bars, 50 µm. Source data are provided as a Source Data file.

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