Through a novel approach using data sonification, researchers have uncovered how hydrogen bonds influence protein folding. This auditory method revealed key patterns and transitions in the folding process, offering insights that surpass visual data analysis and enhancing understanding of diseases linked to protein misfolding. Credit: SciTechDaily.com
“A protein must fold properly to become an enzyme or signaling molecule or whatever its function may be — all the many things that proteins do in our bodies,” said University of Illinois Urbana-Champaign chemistry professor Martin Gruebele, who led the new research with composer and software developer Carla Scaletti.
A sonification and animation of a state machine based on a simple lattice model used by Martin Gruebele to teach concepts of protein-folding dynamics. Video summary for the research “Hydrogen bonding heterogeneity correlates with protein folding transition state passage time as revealed by data sonification” published in PNAS May 21, 2024 vol. 121 no. 21, DOI: https://doi.org/10.1073/pnas.2319094121