Again in E. coli, a misfolded protein is ensconced in an example of these proteins, GroEL, which is capped by GroES, another example of them.
The small type of these proteins contains a conserved alpha-crystallin domain. In E. coli, sigma 32 replaces sigma 70 in RNA polymerase to upregulate these proteins. The activity of an example of these proteins is regulated by a cofactor with a J domain. Again in E. coli, a misfolded protein is ensconced in an example of these proteins, GroEL, which is capped by GroES, another example of them. These proteins are mostly suffixed by their weight in kilodaltons, like the 70, 90, and 100 types. The best studied class of these proteins acts as molecular chaperones. For 10 points, identify these proteins that are part of the response to an increase in cell temperature.
The small type of these proteins contains a conserved alpha-crystallin domain.
Hsps [or heat shock proteins; or heat stress proteins; or molecular chaperone proteins or chaperonins until "chaperones" is read]