The dynamic dimer structure of the chaperone Trigger Factor
The bacterial chaperone Trigger Factor (TF) is a dynamic protein and its dimer structure is unknown. Here the authors present a protocol combining NMR, computational and biophysical methods for the structural characterization of large dynamic protein complexes and show that TF forms a symmetric head...
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2017-12-01
|
| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-017-02196-7 |