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Exact(6)
The critical protein-to-lipid ratio x tilt is the same as in the previous case.
In all the cases we studied we obtained x tilt > x ∗ c.
According to our calculations, for both endophilin WT and amphiphysin N-BAR domains the relationship between the critical molar ratios is x ∗ c < x tilt.
This means that in the whole range of stability of the tubular phase x < x tilt the scaffold orientation is perpendicular to the cylinder axis.
Repeating the same procedure as in the case of rigid scaffolds we find again that at low protein-to-lipid ratios x < x tilt the free energy of the system is minimized at ψ = π / 2 and at high concentrations of N-BARs, x > x tilt, the scaffolds attain a tilted orientation.
The kink in the curve corresponds to the critical protein-to-lipid ratio x tilt ≈5.3·10−3 for which the orientation of the scaffolds on the membrane starts deviating from π / 2. The proposed criterion for tilting J s (x tilt ) = C p is satisfied in this case.
Similar(54)
We found a difference in rotation of the cup around the x-axis (tilt) between the 2 groups.
*Tilt (x) stands for tilt around x-axis (superior/inferior tilt).
When the angle (2θ − Ω) is small, the angular acceptance region in reciprocal space, defined by ΔX, will accept intensity over a wide range of tilt X of the sample.
This path difference leads to the amplitude for a stack of parallel planes being This is a combination of the separation between the planes, d, and the number in the stack, N, and the incident angle, which is given as Ω0 to refer to the case when there is no tilt, X = 0.
The residual can be expressed as R i, j, k axial + tilt (d X, d Y ) = I X (x i, y j, z k + δ z X (y j ) + x i m X (y j ) ) − I Y (x i, y j, z k + δ z Y (x i ) + y j m Y (x i ) ) (9 where m X (y j ) and m Y (x i ) are parameters that model per B-scan axial slopes that represent tilting.
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