Fig. 3: Effects of phosphorylation on predicted residue-wise fluctuations and normal modes of motion.
From: Global comparative structural analysis of responses to protein phosphorylation
a Diagram illustrating various aspects of protein dynamics under study. b Example of clear local changes in residue fluctuations upon phosphorylation. c Pie chart categorizing the types of local changes in dynamics. d Similarity of matching normal modes between phosphorylated and non-phosphorylated proteins over four different frequency windows (from slowest to fastest), stratified by overall similarity on the first 20 modes. G global, LF low frequency, LTIF low to intermediate frequency, HF high frequency. Shaded bands indicate 95% confidence intervals of the median similarity. e, f Two different examples of changes in normal modes. Above: elongation factor Tu 1 from E. coli (UniProt ID P0CE47). Below: human aurora kinase A, (UniProt ID O14965). Heatmaps show all pairwise similarities (as RMSIPs) between the 20 lowest frequency modes; yellow asterisks highlight a normal mode of the same relative frequency but with clear differences between phosphorylated and non-phosphorylated structures. Vector field plots show the highlighted normal modes of the same relative frequency for non-phosphorylated (left) and phosphorylated structures (right). Arrow length proportional to the magnitude of fluctuations (for clarity, scaled differently above and below). Phosphosite indicated in green spheres. The protein icon (credited to Database Center for Life Science) and the heatmap icon (credited to Chenxin Li) in panel a are from Bioicons (bioicons.com) and are under the CC BY 4.0 license. Source data are provided as a Source Data file.
