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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“The history is always the same the product is always different and the history interests more than the product. More, that is, more. Yes. But if the product was not different the history which is the same would not be more interesting.”
—Gertrude Stein (1874–1946)
“A man acquainted with history may, in some respect, be said to have lived from the beginning of the world, and to have been making continual additions to his stock of knowledge in every century.”
—David Hume (1711–1776)
“Anything in history or nature that can be described as changing steadily can be seen as heading toward catastrophe.”
—Susan Sontag (b. 1933)