Fig. 2 Dynamics of Im7 protein by backbone 15N-NMR spin relaxation and molecular dynamics (MD) simulations. Dynamics of Im7 protein by backbone 15N-NMR.

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Fig. 2 Dynamics of Im7 protein by backbone 15N-NMR spin relaxation and molecular dynamics (MD) simulations. Dynamics of Im7 protein by backbone 15N-NMR spin relaxation and molecular dynamics (MD) simulations. (A) 15N-R2 relaxation rates measured in the absence (gray) and presence (black) of NPs. Data points with asterisks (*) indicate substantial chemical exchange Rex effects. (B) R2 differences (ΔR2) of (A) with secondary structure of Im7 indicated at the bottom (4 α helices and 310 helix at N terminus). Experimental uncertainty (1 SD) is depicted by the shaded red area based on five independently measured ΔR2 profiles (see fig. S6). (C) Comparison of ΔR2-derived S2 (red circles) with standard model-free S2 order parameters (blue circles) and S2 values determined from 1-μs MD trajectory with variable averaging time window (from 250 ps to 1 μs). (D) S2(ΔR2) values mapped on three-dimensional (3D) crystal structure [Protein Data Bank (PDB) code 1AYI] show loops and tails that undergo substantial dynamics on pico- to microsecond time scales. N.A., not available. Mouzhe Xie et al. Sci Adv 2019;5:eaax5560 Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).