Chaperone function of two small heat shock proteins from maize

- Two 17-kDa small heat shock proteins from Zea mays differ in chaperone capability.
- Very similar sequence except for a 9-amino acid intervening sequence at the N-terminus.
- Intervening sequence may force structural changes in a partly disordered domain.
- Dodecamers (shown in TEM images) dissociate to smaller oligomers during heat shock.
- Larger protein is a significantly better chaperone during heat shock.