Related Experiment Video
Updated: Jun 2, 2026

Exploring Protein-Glycan Interactions: Advances in Nuclear Magnetic Resonance
Published on: August 26, 2025
Vibrational softening of a protein on ligand binding
Erika Balog1, David Perahia, Jeremy C Smith
1Department of Biophysics and Radiation Biology, Faculty of Medicine, Semmelweis University, Budapest, Hungary.
Abstract:
Neutron scattering experiments have demonstrated that binding of the cancer drug methotrexate softens the low-frequency vibrations of its target protein, dihydrofolate reductase (DHFR). Here, this softening is fully reproduced using atomic detail normal-mode analysis. Decomposition of the vibrational density of states demonstrates that the largest contributions arise from structural elements of DHFR critical to stability and function. Mode-projection analysis reveals an increase of the breathing-like character of the affected vibrational modes consistent with the experimentally observed increased adiabatic compressibility of the protein on complexation.
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