(
A) Schematic depiction of pQa-1-SCT. A disulfide-trapped version (dtSCT) was made by substitutions of Linker1 G2C and pQa-1 Y84C. Surface expression of pQa-1-SCT on CHO cells was compared with pQa-1 (left) or with pQa-1-dtSCT (right) by FACS analysis. (
B) Thermostability of pQa-1-SCT or pQa-1-dtSCT was measured by circular dichroism (CD) as described (
Mitaksov et al., 2007). The increase in the CD signal at 220 nm as a function of temperature was normalized on a scale of 0 to 100. The T
m for each protein is denoted in the legend. For these thermal denaturation studies, purified pQa-1-SCT proteins were dialyzed against buffer containing 10 mM K
2HPO
4/KHPO
4pH = 7.5 and 150 mM NaCl, and diluted to 475 nM in buffer containing 20 mM K
2HPO
4/KHPO
4pH = 7.5 and 150 mM NaCl. Circular dichroism (CD) spectra at 10°C were collected between 260 and 200 nm at 0.5 nm increments on a Jasco-810 instrument (Jasco Inc., Easton MD) equipped with a Peltier temperature controller. The thermal denaturation profiles were monitored by the change in CD signal at 220 nm as a function of temperature. Thermal scan data were collected at 1.0°C intervals from 10°C to 70°C with a temperature ramp rate of 50 °C/hour. Thermal denaturation curves were scaled from 0% to 100% to provide plots of the percent of signal change versus temperature. The T
m is the temperature at which the CD signal change is half of the total signal change. All measurements were made at least four times and averaged.