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Characterization of HSA unfolding at room temperature. (A) Tryptophan fluorescence blue-shifts upon reduction by DTT, characteristic of HSA unfolding. (B) Far-UV CD spectrum of folded HSA shows minima at 208 and 222 nm, characteristic of a-helical proteins; the helix peaks decrease on addition of DTT, indicating substantial unfolding of HSA. (C) Second derivative ATR-FTIR spectrum shows a decrease of the helix bands and no aggregation of unfolded HSA.
