[HTML][HTML] Oligomeric structure and chaperone-like activity of Drosophila melanogaster mitochondrial small heat shock protein Hsp22 and arginine mutants in the alpha …
A Dabbaghizadeh, S Finet, G Morrow… - Cell Stress and …, 2017 - Elsevier
The structure and chaperone function of DmHsp22WT, a small Hsp of Drosophila
melanogaster localized within mitochondria were examined. Mutations of conserved
arginine mutants within the alpha-crystallin domain (ACD) domain (R105G, R109G, and
R110G) were introduced, and their effects on oligomerization and chaperone function were
assessed. Arginine to glycine mutations do not induce significant changes in tryptophan
fluorescence, and the mutated proteins form oligomers that are of equal or smaller size than …
melanogaster localized within mitochondria were examined. Mutations of conserved
arginine mutants within the alpha-crystallin domain (ACD) domain (R105G, R109G, and
R110G) were introduced, and their effects on oligomerization and chaperone function were
assessed. Arginine to glycine mutations do not induce significant changes in tryptophan
fluorescence, and the mutated proteins form oligomers that are of equal or smaller size than …