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APPLICATION NOTE
Figure 2: Interaction of RTA with P1-P2 protein complexes. (A) MST binding curves for the P1-P2, P1-P2ΔC and P1ΔC-P2 complexes with RTA. (B) MST binding curves for
the P2-P2, P2ΔC-P2ΔC and P1ΔC-P2ΔC and RTA. To obtain ΔFnorm, the baseline Fnorm value is subtracted from all data points of the same curve. Thus, by definition,
ΔFnorm is 0 in the unbound state. Error bars ± SE (n = 3).
Protein complex MST SPR BLI ITC
P1-P2 K
d
= 86nM
Interaction visible, slow
K
off
, no fit possible
K
d
= 21nM Binding, low C value
P1-ΔP2 K
d
= 533nM K
d
= 90nM Binding, low C value
P2-P2 K
d
= 1-2µM Slow K
off
, no fit possible K
d
= 2µM No saturation, low C value
ΔP1-P2 No interaction No interaction No saturation No saturation, low C value
ΔP1-ΔP2 No saturation No interaction No saturation No saturation, low C value
ΔP2-ΔP2 No interaction No interaction No clear interaction No saturation, low C value
Table 1: Summary of trimeric complex molecular interaction characterization with various biophysical techniques
A
B
