The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy
Solution NMR provides an information-rich technique to monitor the unfolding process and probe the heterogeneity of protein unfolding. Differences in unfolding dynamics of core and peripheral residues during the cold denaturation of Yfh1 are followed in the present study by 1H-15N HSQC spectroscopy.
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2021-09-01
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| Series: | Communications Chemistry |
| Online Access: | https://doi.org/10.1038/s42004-021-00566-3 |