. Author manuscript; available in PMC: 2014 Jan 27.

Published in final edited form as: Biochemistry. 2012 May 1;51(19):4062–4071. doi: 10.1021/bi300243z

Table 1.

Thermal unfolding temperatures for different IpaB N-terminal domain proteins with and without IpgC.

Protein	T_m (°C)^a
IpgC	45.0
IpaB^28.226	57.5
IpaB^1.226	57.5
IpaB^1.226/IpgC	45.0/60.0^b
IpaB^1.94/IpgC	62.5

The CD signal at 222 nm was monitored for each protein as a function of temperature from 10–85°C. Spectra were collected every 2.5°C with 5 min allowed for temperature equilibration.

The midpoint of thermal unfolding (given as T_m) was determined as an indicator of transition from a folded to unfolded state. The standard error in each case is less than 2°C.

This protein pair appeared to have two unfolding transitions, which in this case could represent a separation of the two proteins followed by observation of their individual unfolding transitions.