Table 1.

The kinetic model of BlaR^s acylation and the ensuing protein conformational changes at 22°C, 10°C, and 5°C

t, °C	kacyl, s−1	First conformational change		Second conformational change
		kc1, s−1	ΔA‡	kc2, s−1	ΔA‡
22	>10	>10	+0.04	3.1 ± 0.3	−0.02
10	3.8 ± 0.8	1.0 ± 0.05	+0.005, +0.035§	0.030 ± 0.004	−0.005
5	0.6 ± 0.1	0.80 ± 0.07	+0.05	0¶	0¶

*The value for K_s at room temperature is 23 μM (2).

^†The rate constants measured for changes in the α-helix and β-sheet content are identical.

^‡The magnitude of the IR absorbance change under the experimental conditions.

^§The first value is the kinetically observed part of the change. The second value is the total absorbance change.

^¶Under the conditions of the experiment (length of observation at 5°C), this conformational change does not occur.