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. 2002 Mar;11(3):680–687. doi: 10.1110/ps.22202

Fig. 4.

Fig. 4.

Thermal unfolding of the VHP subdomain mutants monitored by CD at 222 nm. (a) Single mutants. (b) Double mutants. Samples were 40 to 60 μM protein in 50 mM phosphate buffer, pH 7.0. For clarity, only every fourth data point is shown. For reference, the thermal unfolding of M53L is repeated in plot (b). HP36 (+); M53L (filled diamonds); F47L (open circles); F51L (open squares); F58L (open triangles); F47,51L (filled triangles); F47,58L (filled squares); F51,58L (filled circles).