Extended Data Fig. 10: pH- and BMP-dependent binding of Rho-ZF5.3 to large unilamellar vesicles is observed via fluorescence anisotropy. | Nature Chemistry

Extended Data Fig. 10: pH- and BMP-dependent binding of Rho-ZF5.3 to large unilamellar vesicles is observed via fluorescence anisotropy.

From: The biophysical requirements that govern the efficient endosomal escape of designed mini-proteins

Extended Data Fig. 10: pH- and BMP-dependent binding of Rho-ZF5.3 to large unilamellar vesicles is observed via fluorescence anisotropy.The alternative text for this image may have been generated using AI.

a, Equilibrium binding curves of BMP + LE/LY LUVs and b, BMP − LE/LY LUVs to 100 nM Rho-ZF5.3 and Rho-BBA5.3 at pH 4.5 and 7.5. Each point represents the mean ± SEM of anisotropy, n = 3 replicate wells.

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