Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered p...
Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes
About this item
Full title
Author / Creator
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
Formats
Publication information
Publisher
London: Nature Publishing Group UK
Subjects
More information
Scope and Contents
Contents
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 interaction exhibits another surprising feature: The association...
Alternative Titles
Full title
Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_64b405d60211411596d26e2756ae1e36
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_64b405d60211411596d26e2756ae1e36
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-020-18859-x
