A study published in Nature Chemistry investigates how the environment reshapes protein conformational energy landscapes using the model protein GB1. In this project, led by Paul Schanda’s group at ISTA in collaboration with the Synchrotron group at IBS, the researchers compared its dynamics in solution, in a crystal, and when bound to its partner IgG. Using NMR, they showed that some buried aromatic rings flip nearly a thousand times more slowly in crystals than in solution. In contrast, these motions can be strongly accelerated when GB1 interacts with IgG. These results demonstrate how intermolecular contacts can profoundly reshape a protein’s dynamic energy landscape. The GB1 crystal structures under cryogenic and room-temperature conditions were determined on beamlines BM07-FIP2 and ID30B at the ESRF. By combining crystallography, NMR and molecular dynamics simulations, the study provides a more complete picture of how proteins “breathe”.
Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes. Becker LM, Fu H, Tatman BP, Dreydoppe M, Kapitonova A, Balazs DM, Weininger U, Engilberge S, Chipot C, Schanda P. Nature Chemistry 2026 ; 18(7):1221-1230. https://www.nature.com/articles/s41557-026-02155-
IBS Contact : Sylvain Engilberge, IBS/Synchrotron Group