Heat shock proteins are intracellular molecular chaperones.
HSPs are molecular chaperones that specifically prevent irreversible protein aggregation (Waters 2013).
Hsp100 family of molecular chaperones shows a unique capability to resolubilize and reactivate aggregated proteins.
Molecular chaperones were co-expressed with rLF to facilitate its correct folding.
In vivo, folding of these proteins is mediated by molecular chaperones.
Heat shock proteins (HSPs) are an evolutionary family of proteins that act as molecular chaperones.
Heat shock proteins 70 (HSP70s) are molecular chaperones that aid in protection against environmental stress.
In addition to enzymic activity, many immunophilins act as molecular chaperones.
Water molecules and molecular chaperones efficiently help the protein folding process.
Molecular chaperones stimulate the immune system to induce both protective immune responses and therapeutic tumor rejection.
Molecular chaperones also regulate protein localization and protein-protein interactions, thereby contributing to functional protein networks [5].
