| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2017088 | Plant Science | 2014 | 11 Pages |
Abstract
- 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.
Keywords
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Plant Science
Authors
Roger D. Klein, Tamutenda Chidawanyika, Hannah S. Tims, Tea Meulia, Robert A. Bouchard, Virginia B. Pett,