History
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 ability of a nuclear protein called nucleoplasmin to prevent the aggregation of folded histone proteins with DNA during the assembly of nucleosomes. The term was later extended by R. John Ellis in 1987 to describe proteins that mediated the post-translational assembly of protein complexes. In 1988, it was realised that similar proteins mediated this process in both prokaryotes and eukaryotes. The details of this process were determined in 1989, when the ATP-dependent protein folding was demonstrated in vitro.
Read more about this topic: Chaperone (protein)
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“Gossip is charming! History is merely gossip. But scandal is gossip made tedious by morality.”
—Oscar Wilde (1854–1900)
“We aspire to be something more than stupid and timid chattels, pretending to read history and our Bibles, but desecrating every house and every day we breathe in.”
—Henry David Thoreau (1817–1862)