Dynamic protein structures in solution: decoding the amide I band with 2D-IR spectral libraries and machine learning
The dynamic three-dimensional structures of proteins dictate their function, but accessing structures in solution at physiological temperatures is challenging. Ultrafast 2D-IR spectroscopy of the protein amide I band produces a spectral fingerprint that derives directly from the 3D backbone structure within minutes, using microlitres of label-free samples, in aqueous (H<sub>2</sub>O) solution and with picosecond time resolution. However, transforming 2D-IR fingerprints into quantitative, solution-phase protein structures relies on decoding the fundamental link between the atomistic structure and the 2D spectrum. We demonstrate a top-down approach to solution-phase protein structure determination that combines 2D-IR spectral libraries with machine learning (ML). Using a dataset consisting of 6732 spectra of 35 proteins in H<sub>2</sub>O that span a range of structures, Support-Vector Machine (SVM) models classified unknown protein samples according to structural content and measured quantities of α-helix and β-sheet with an RMS error of ≤7%. The potential for hybrid 2D-IR-ML tools to predict the number and length of helices in a protein, and identify the presence of parallel and antiparallel β-sheets from the 2D-IR fingerprint is also demonstrated. These results lay the groundwork for rapid, quantitative analysis of dynamic protein structures under physiologically relevant conditions.
Authors
- Neil T. Hunt (ORCID: https://orcid.org/0000-0001-7400-5152)
- Gregory M. Greetham (ORCID: https://orcid.org/0000-0002-1852-3403)
- Amy Farmer (ORCID: https://orcid.org/0009-0007-4154-9664)
- Kelly Brown
- Sophie E.T. Kendall-Price
- Partha Malakar
Institutions
- Research Complex at Harwell (GB)
- University of York (GB)
Publication Details
- Journal
- Chemical Science
- Published
- 2026-01-01
- DOI
- https://doi.org/10.1039/d5sc09973k
- Primary Topic
- Spectroscopy and Quantum Chemical Studies
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Engineering and Physical Sciences Research Council
- Science and Technology Facilities Council
- Central Laser Facility, Science and Technology Facilities Council