Ontology highlight
ABSTRACT:
SUBMITTER: Salmon L
PROVIDER: S-EPMC5738273 | biostudies-literature | 2018 Jan
REPOSITORIES: biostudies-literature
Salmon Loïc L Stull Frederick F Sayle Sabrina S Cato Claire C Akgül Şerife Ş Foit Linda L Ahlstrom Logan S LS Eisenmesser Elan Z EZ Al-Hashimi Hashim M HM Bardwell James C A JCA Horowitz Scott S
Journal of molecular biology 20171111 1
HdeA is a periplasmic chaperone that is rapidly activated upon shifting the pH to acidic conditions. This activation is thought to involve monomerization of HdeA. There is evidence that monomerization and partial unfolding allow the chaperone to bind to proteins denatured by low pH, thereby protecting them from aggregation. We analyzed the acid-induced unfolding of HdeA using NMR spectroscopy and fluorescence measurements, and obtained experimental evidence suggesting a complex mechanism in HdeA ...[more]