Quantitative prediction of ensemble dynamics, shapes and contact propensities of intrinsically disordered proteins
Fig 3
Back-calculated R1, R2 NMR 15N-spin relaxation rates in comparison with experiment along with underlying motional time-scale distributions.
R1, R2 rates calculated from average correlation functions are plotted in blue with error bars representing standard deviations across individual MD trajectories. Correlation time distribution of individual 15N-1H bonds of IDPs extracted from correlation functions for (E) p53TAD and (F) Pup where the sizes of the blue squares are proportional to the associated motional amplitudes Ai. The squares at the bottom indicate the aggregate of dynamics contributions with correlation times faster than 100 ps. Dominant dynamics time scales range from about 100 ps to about 10 ns depending on the residue, with the exception of Thr12 in Pup which exhibits dominant dynamics time scales faster than 100 ps.