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. 2015 Dec 16;7(3):1933–1939. doi: 10.1039/c5sc02900g

Fig. 2. Thermal denaturation profile of UapA protein purified in DDM and then exchanged into novel TDTs (a) and NDTs (b) at detergent concentrations of CMC + 0.04 wt%. Thermal stability of the protein was monitored by CPM assay performed at 40 °C for 120 min. The relative amounts of folded protein were normalized relative to the most destabilizing condition in this experiment, that is, protein denaturation in DDM after 2 h incubation. Mean standard deviations (n = 2) for DDM, TDT-C9, TDT-C10, TDT-C11, TDT-C12, NDT-C9, NDT-C10, NDT-C11 and NDT-C12 are 4.9, 9.3, 2.3, 5.8, 6.1, 2.7, 9.4, 10.2, 9.5, respectively.

Fig. 2