Regulation of chaperone function by coupled folding and oligomerization
Guillaume Mas, Björn M. Burmann, Timothy Sharpe, Beatrice Claudi, Dirk Bumann, Sebastian Hiller
Abstract
fitness in a mouse infection model. The coupled mechanism is a unique example of how an ATP-independent chaperone can modulate its activity as a function of the presence of client proteins.
Topics & Concepts
Chaperone (clinical)BiophysicsProtein foldingCo-chaperoneCell biologyFolding (DSP implementation)Function (biology)ChemistryComputational biologyBiological systemBiologyBiochemistryHsp90Heat shock proteinMedicineEngineeringElectrical engineeringGenePathologyHeat shock proteins researchToxin Mechanisms and ImmunotoxinsEnzyme Structure and Function