PMC

a Histograms of delta values (d1 and d2) in DLPFC area for order 1 and order2. b Histograms of theta values (d1 and d2 values) in DLPFC area for order 1 and order 2. c Delta power representation (d1 and d2 values) for order 1 and 2. The red color represents the areas in which compare an increase of delta d1 and d2 values. d Theta power representation (d1 and d2 values) for order 1 and 2. The figure shows an increase of theta in DLPFC area for order 1 than order 2. The blue color represents the areas in which compare an increase of theta d1 and d2 values. e Histogram of alpha values (d1 values) in DLPFC area for order 1 and order 2. f Histogram of alpha values (d2 values) in DLPFC area for order 1 and order 2

a The two intertwined order parameters Δ₀ (superconducting) and Q₀ (nematic). b The anisotropic diamagnetic susceptibilities χ_xx, χ_yy and χ_zz together with the experimental magnetization data on a log-linear scale to compare with the theory.

(A) The relationship between the average order parameter in distant, non-solvent-exposed residues versus the average order parameters in binding site residues (n = 743, slope = 0.79, r² = 0.65; p=6.5 × 10^–89, two-sided t-test). (B) We compare the difference in order parameters in each binding site residues of holo-apo pairs compared to a control dataset made up of the same number, type, and solvent exposure of amino acids. Comparing the apo/holo structures, on average binding site residues got more rigid upon binding. The median difference in order parameters was 0.03 for the binding site residues compared to 0 for the control dataset (p=3.4 × 10^–7, individual Mann–Whitney U test). (C) The relationship between the residual order parameters in all distant residues versus binding site residue order parameters (n = 743, slope = −0.34, r² = 0.17; p=4.6 × 10^–28, two-sided t-test). (D) The relationship between the residual order parameters in distant, non-solvent-exposed residues versus binding site residues in the apo and apo control dataset residues (n = 283, slope = −0.28, r² = 0.20; p=1.8 × 10^–34, two-sided t-test). (E) To analyze the impact that protein size has on the relationship between the difference in order parameters in binding site residues versus the residual order parameters in distant residues, we binned proteins based on the number of residues. We colored each point on our original binding site residues versus the residual order parameters in distant residues based on the protein size and did not observe any clustering. (F) The bootstrap analysis of the overlap of the slope of distant, average order parameters of non-solvent-exposed residue versus average order parameters of binding site residue between holo-apo (green) and apo-apo (purple). While there was some overlap, the mean slope of holo-apo (–0.44) was more than 2 standard deviations away from the mean slope of the apo-apo (–0.28). Comparing the two bootstrap distributions using a z-test, the z-value was –191.26 with a p-value of 0.0.

The observed ranking order for the example session of observer JW plotted as a “depth map” (regions are Voronoi cells, gray level denotes rank order). Lighter means closer. Compare the stimulus picture at right. Notice (left) that the scene roughly divides into foreground, middle ground, and background.