The '''Chaperone code''' refers to modifications of molecular chaperones that control protein folding. WhileWhilst the [[genetic code]] specifies how DNA makes proteins, whileand the [[histone code]] rulesregulates genomichistone-DNA transactionsinteractions, the chaperone code controls how proteins are folded to produce a functional [[proteome]].<ref name=":0">{{Cite journal|last=Nitika|last2=Porter|first2=Corey M.|last3=Truman|first3=Andrew W.|last4=Truttmann|first4=Matthias C.|date=2020-07-31|title=Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code|url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7397107/|journal=The Journal of Biological Chemistry|volume=295|issue=31|pages=10689–10708|doi=10.1074/jbc.REV120.011666|issn=0021-9258|pmc=7397107|pmid=32518165}}</ref><ref>{{Cite journal|last=Backe|first=Sarah J.|last2=Sager|first2=Rebecca A.|last3=Woodford|first3=Mark R.|last4=Makedon|first4=Alan M.|last5=Mollapour|first5=Mehdi|date=2020-08-07|title=Post-translational modifications of Hsp90 and translating the chaperone code|url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7415980/|journal=The Journal of Biological Chemistry|volume=295|issue=32|pages=11099–11117|doi=10.1074/jbc.REV120.011833|issn=0021-9258|pmc=7415980|pmid=32527727}}</ref>
The chaperone code refers to the combinatorial array of post-translational modifications (enzymes add chemical modifications to amino acids that change their properties) - i.e. phosphorylation, acetylation, ubiquitination, methylation, etc - that are added to [[molecular chaperones]] to modulate their activity. Molecular chaperones are proteins specialized in folding and unfolding of the other cellular proteins, and the assembly and dismantling of protein complexes. This is critical in the regulation of protein-protein interactions and many cellular functions.
