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Resolving the conformational ensemble of a membrane protein by integrating small-angle scattering with AlphaFold

Fig 3

Change in experimental SANS profiles corresponds to the difference between generated states.

(A, B) Theoretical and experimental SANS curves at resting (pH 7.5) and activating (pH 3.0) conditions of the predicted GLIC conformational states for scattering vectors Å⁻¹ (A) and Å⁻¹ (B). Error-normalized residuals are shown below. (C) Experimental and theoretical SANS difference curves between activating and resting conditions as well as between the open and closed prediction, with the latter scaled to fit the former. An error-normalized residual is shown below. (D) Fit of the predicted versus experimental difference curves as a function of the population shift from the closed prediction to open prediction. The dashed line indicates the optimal fit, and corresponds to a 30% increase in the contribution of the predicted open versus closed states.

doi: https://doi.org/10.1371/journal.pcbi.1013187.g003