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Access through your institution Buy or subscribe Both the editorial in this issue of _Nature Structural Biology_ and the paper on page 1132 focus on protein folding research. Here we note
that our understanding of the general properties of folding reactions _in vivo_ took a major step forward in the late 1980s, when research from several disparate fields revealed the
widespread function of the GroEL (hsp60) related proteins, members of the class of chaperones known as the chaperonins. GroEL is required for the correct assembly of the oligomeric structure
that connects the head to the tail of λ phage. It was identified in 1972–1973 by genetic approaches, in the search for factors involved in the replication of bacteriophages1,2 and its name
reflects this history: 'Gro' stands for phage growth; 'E' indicates that the growth defect can be overcome by a mutation in the phage head gene E; and 'L'
stands for 'large subunit'. This is a preview of subscription content, access via your institution ACCESS OPTIONS Access through your institution Subscribe to this journal Receive
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Osterman, J., Horwich, A.L., Neupert, W. & Hartl, F.-U. _ Nature_ 341, 125–130 ( 1989). Article Google Scholar Download references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Tracy
Smith Authors * Tracy Smith View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS
ARTICLE Smith, T. The discovery of chaperonins. _Nat Struct Mol Biol_ 6, 1090 (1999). https://doi.org/10.1038/70015 Download citation * Issue Date: December 1999 * DOI:
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