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. 2018 Jun 28;138(3):303–313. doi: 10.1007/s11120-018-0544-6

Table 2.

Kd values of protein–protein interactions within the posttranslational cpSRP-pathway of Arabidopsis thaliana

Interaction Method Kd [µM] References
cpSRP43/Alb3
 43/Alb3 C-terminus FA 12–18 Liang et al. (2016)
 43/Alb3 C-terminus ITC 5.1 Horn et al. (2015)
 43/Alb3 C-terminus ITC 9.7–13.2 Falk et al. (2010); Falk and Sinning (2010a, 2010b)
 43/Alb3 C-terminus ITC 0.094 Lewis et al. (2010)
cpSRP43/LHCP
 43/LHCP LS 0.17/1.5 Liang et al. (2016)
 43/LHCP + 54M 0.26
 43/LHCP FA 0.14–0.3 Jaru-Ampornpan et al. (2010)
 43/L18 ITC 0.322 Gao et al. (2015)
 43/L18 + RRKRp10 0.107
 43/L18 ITC 1.17 Stengel et al. (2008)
 43/L11 FA 0.022 Liang et al. (2016)
 43/L11 + Alb3 C-terminus 0.011
cpSRP43/cpSRP54
 43/54 MST 0.05 Ziehe et al. (2016)
 43/54 FCS 0.095 Gao et al. (2015)
 43/54M SPR 0.0025 Hermkes et al. (2006)
cpSRP54/cpFtsY
 54/FtsY - PG FRET 2.34 Chandrasekar and Shan (2017)
 54/FtsY + PG 0.13
 54/FtsY* FRET 0.77 Chandrasekar et al. (2017)
 54NG/FtsY* 12

Enlisted are the dissociation constants (Kd values) of protein complexes of the posttranslational cpSRP-pathway. Additionally, the methods by which the Kd values were determined as well as possible variations of the experimental settings are shown

FA fluorescence anisotropy, FCS fluorescence correlation spectroscopy, FRET forster resonance energy transfer, ITC isothermal titration calorimetry, LA light scattering, MST microscale thermophoresis, SPR surface plasmon resonance spectroscopy

* measured in the presence of 0.01 % Nikkol (mimicking of the effect of lipids)