Structure and function of small heat shock/α-crystallin proteins: established concepts and emerging ideas

@article{MacRae2000StructureAF,
  title={Structure and function of small heat shock/α-crystallin proteins: established concepts and emerging ideas},
  author={Thomas H MacRae},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={2000},
  volume={57},
  pages={899-913}
}
Small heat shock/α-crystallin proteins are defined by a conserved sequence of approximately 90 amino acid residues, termed the α-crystallin domain, which is bounded by variable amino- and carboxy-terminal extensions. These proteins form oligomers, most of uncertain quaternary structure, and oligomerization is prerequisite to their function as molecular chaperones. Sequence modelling and physical analyses show that the secondary structure of small heat shock/α-crystallin proteins is… CONTINUE READING