In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There … See more

In human cell lines, chaperone proteins were found to compose ~10% of the gross proteome mass, and are ubiquitously and highly expressed across human tissues.
Chaperones are found extensively in the endoplasmic reticulum (ER), since protein synthesis See more

The genes of bacteriophage (phage) T4 that encode proteins with a role in determining phage T4 structure were identified using conditional lethal mutants. Most of these … See more

There are many disorders associated with mutations in genes encoding chaperones (i.e. multisystem proteinopathy) that can affect muscle, bone … See more

Many chaperones are heat shock proteins, that is, proteins expressed in response to elevated temperatures or other cellular stresses. Heat shock protein chaperones are classified based on their observed molecular weights into Hsp60, Hsp70, Hsp90, Hsp104, … See more

There are many different families of chaperones; each family acts to aid protein folding in a different way. In bacteria like E. coli, many of these proteins are highly expressed under conditions of high stress, for example, when the bacterium is placed in high … See more

The investigation of chaperones has a long history. The term "molecular chaperone" appeared first in the literature in 1978, and was invented by Ron Laskey to describe the … See more