Abstract
The vibrational coupling between protein backbone modes and the role of water interactions are important topics in biomolecular spectroscopy. Our work reports the first study of the coupling between amide I and amide A modes within peptides and proteins with secondary structure and water contacts. We use two-color two-dimensional infrared (2D IR) spectroscopy and observe cross peaks between amide I and amide A modes. In experiments with peptides with different secondary structures and side chains, we observe that the spectra are sensitive to secondary structure. Water interactions affect the cross peaks, which may be useful as probes for the accessibility of protein sites to hydration water. Moving to two-color 2D IR spectra of proteins, the data demonstrate that the cross peaks integrate the sensitivities of both amide I and amide A spectra and that a two-color detection scheme may be a promising tool for probing secondary structures in proteins.
| Original language | English |
|---|---|
| Journal | The Journal of Physical Chemistry Letters |
| Volume | 15 |
| Issue | 18 |
| Pages (from-to) | 4933-4939 |
| Number of pages | 7 |
| ISSN | 1948-7185 |
| DOIs | |
| Publication status | Published - May 2024 |
Keywords
- Amides/chemistry
- Peptides/chemistry
- Protein Structure, Secondary
- Proteins/chemistry
- Spectrophotometry, Infrared/methods
- Water/chemistry