Abstract
Diffusion of proteins on length scales of their size is crucial for understanding the machinery of living cells. X-ray photon correlation spectroscopy (XPCS) is currently the only way to access long-time collective diffusion on these length scales, but radiation damage so far limits the use in biological systems. We apply a new approach to use XPCS to measure cage relaxation in crowded α-crystallin solutions. This allows us to correct for radiation effects, obtain missing information on long time diffusion, and support the fundamental analogy between protein and colloid dynamical arrest.
| Original language | English |
|---|---|
| Article number | 238001 |
| Number of pages | 6 |
| Journal | Physical Review Letters |
| Volume | 129 |
| Issue number | 23 |
| DOIs | |
| Publication status | Published - 2022 Dec 2 |
Subject classification (UKÄ)
- Physical Chemistry (including Surface- and Colloid Chemistry)
- Biophysics