Probing Protein Dynamics Using Multifield Variable Temperature NMR Relaxation and Molecular Dynamics Simulation

• Published in: The journal of physical chemistry. B Vol. 122; no. 42; pp. 9697 - 9702
• Main Authors: Busi, Baptiste, Yarava, Jayasubba Reddy, Hofstetter, Albert, Salvi, Nicola, Cala-De Paepe, Diane, Lewandowski, Józef R, Blackledge, Martin, Emsley, Lyndon
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 25.10.2018
• Subjects: Biochemistry, Molecular Biology; Life Sciences; Structural Biology
• ISSN: 1520-6106; 1520-5207
• DOI: 10.1021/acs.jpcb.8b08578

Understanding the interplay between protein function and dynamics is currently one of the fundamental challenges of physical biology. Recently, a method using variable temperature solid-state nuclear magnetic resonance relaxation measurements has been proposed for the simultaneous measurement of 12 different activation energies reporting on distinct dynamic modes in the protein GB1. Here, we extend this approach to measure relaxation at multiple magnetic field strengths, allowing us to better constrain the motional models and to simultaneously evaluate the robustness and physical basis of the method. The data reveal backbone and side-chain motions, exhibiting low- and high-energy modes with temperature coefficients around 5 and 25 kJ·mol–1. The results are compared to variable temperature molecular dynamics simulation of the crystal lattice, providing further support for the interpretation of the experimental data in terms of molecular motion.