Editing Protein tertiary structure (section)

=== Chaperone proteins ===
It is commonly assumed that the native state of a protein is also the most [[thermodynamics|thermodynamically]] stable and that a protein will reach its native state, given its [[chemical kinetics]], before it is [[translation (genetics)|translated]]. Protein [[chaperone (protein)|chaperones]] within the cytoplasm of a cell assist a newly synthesised polypeptide to attain its native state. Some chaperone proteins are highly specific in their function, for example, [[protein disulfide isomerase]]; others are general in their function and may assist most globular proteins, for example, the [[prokaryotic]] [[GroEL]]/[[GroES]] system of proteins and the [[homology (biology)|homologous]] [[eukaryotic]] [[heat shock protein]]s (the Hsp60/Hsp10 system).