Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes
Abstract Highly charged intrinsically disordered proteins can form complexes with very high affinity in which both binding partners fully retain their disorder and dynamics, exemplified by the positively charged linker histone H1.0 and its chaperone, the negatively charged prothymosin α. Their inter...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2020-11-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-18859-x |