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. 2016 Mar 4;15(5):1710–1727. doi: 10.1074/mcp.M116.058131

Table I. ITC measurements of Hsp70/Hsp90-Tomm34 interactions.

ITC was used to investigate the ATP-dependent interaction between Tomm34 and Hsp70. At 25 °C, we observed only a very small enthalpy change for the interaction; thus we explored the interaction at different temperatures (for ITC plots see supplemental Fig. 1). To compare Tomm34 binding to another chaperone, we also measured the Hsp90α/Tomm34 interaction.

Protein complex Nucleotide T KD ΔH ΔS TΔS N
°C μm cal mol1 cal mol1 K1 cal mol1
Hsp70/Tomm34 ATP 5 0.40 ± 0.06 5672 ± 168 49.7 13824 0.43 ± 0.01
Hsp70/Tomm34 ATP 15 0.20 ± 0.05 3625 ± 126 43.3 12477 0.40 ± 0.01
Hsp70/Tomm34a ATP 25 NAb NA NA NA NA
Hsp70/Tomm34 ATP 30 0.10 ± 1.40 −1647 ± 146 26.5 8033 0.60 ± 0.04
Hsp90α/Tomm34 25 0.96 ± 0.10 −6392 ± 146 6.1 1819 0.57 ± 0.01

a It was not possible to analyze the data due to a very small enthalpy change.

b NA means not applicable.