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. Author manuscript; available in PMC: 2018 Feb 5.
Published in final edited form as: J Mol Biol. 2016 Nov 16;429(4):562–573. doi: 10.1016/j.jmb.2016.11.008

Fig. 2.

Fig. 2

Assessing the binding characteristics of RasIn1 in vitro. (a) RasIn1 preferentially binds active (GTP) over inactive (GDP) forms of H-Ras(G12V) (p = 0.007) and preferentially binds unblocked active H-Ras(G12V) as active H-Ras(G12V) blocked with the c-Raf-kinase RBD domain (Raf-RBD; p = 0.002). (b) Binding of RasIn1 to K-Ras is disrupted by the Y32R mutation in the Switch I region (p = 0.03). Error bars indicate the standard deviation of the mean.