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. 2009 Oct 8;28(21):3303–3314. doi: 10.1038/emboj.2009.261

Figure 2.

Figure 2

Comparison of membrane curvature sensing graphs for various BAR domains. Testing the current hypothesis of the molecular mechanism of membrane curvature sensing by BAR domains. All samples are incubated with protein at 40 nM for 1 h unless otherwise stated. (A) Representative members of three BAR domain super families. Surface representation coloured according to electrostatic potential and mesh equipotential surfaces at −5 kT/e to 5 kT/e (blue is +, red is −). Arrows indicate the position of AHs. Neither dimer shape nor electrostatic potential is conserved for the different proteins. (B) Comparison of eNBAR and eNBAR-3KE shows that charge mutations do not alter the ability of this BAR domain to sense membrane curvature. Sensing is identical for eNBAR 3KE at high concentration (5.2 μM). (C) Comparison of eNBAR and oFBAR shows that the intrinsic radius of curvature of the dimer (11 nm versus 65 nm) does not influence membrane curvature sensing. (D) eNBAR shows identical membrane curvature sensing as an IBAR (mIBAR), which has an negative radius of curvature according to the crystal structure. Sensing is identical for mIBAR at high concentration (0.9 μM). Thus, neither charges nor BAR dimer structure is essential for curvature sensing.