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. 1999 Jan 11;144(1):21–30. doi: 10.1083/jcb.144.1.21

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The recombinant C domain folds very stably even in the presence of reducing agents. (A) Recombinant BiP and C domain of λ LC were isolated and examined for purity and folding status. The C domain was incubated for 1 h at 37°C in the presence (+) or absence of DTT and then alkylated with a 10-fold molar excess of NEM. Samples were analyzed by SDS-PAGE under nonreducing conditions. (B) Thermal denaturation curves generated for purified hamster BiP (□) and for the purified C domain under reducing conditions (○). Fraction of native protein remaining was calculated at each temperature.