Abstract
We use infrared spectroscopy to study the evolution of protein folding intermediate structures on arbitrarily slow time scales by rapidly quenching thermally unfolded hen egg white lysozyme in a glassy matrix, followed by reheating of the protein to refold; upon comparison with differential scanning calorimetric experiments, low-temperature structural changes that precede the formation of energetic native contacts are revealed.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 4441-4443 |
| Number of pages | 3 |
| Journal | Chemical Communications |
| Issue number | 29 |
| DOIs | |
| State | Published - 2009 |
All Science Journal Classification (ASJC) codes
- Electronic, Optical and Magnetic Materials
- General Chemistry
- Ceramics and Composites
- Metals and Alloys
- Materials Chemistry
- Surfaces, Coatings and Films
- Catalysis
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