The Dynamics of Hsp25 Quaternary Structure

@article{Ehrnsperger1999TheDO,
  title={The Dynamics of Hsp25 Quaternary Structure},
  author={Monika Ehrnsperger and H. Lilie and M. Gaestel and J. Buchner},
  journal={The Journal of Biological Chemistry},
  year={1999},
  volume={274},
  pages={14867 - 14874}
}
Small heat shock proteins (sHsps), including α-crystallin, represent a conserved and ubiquitous family of proteins. They form large oligomers, ranging in size from 140 to more than 800 kDa, which seem to be important for the interaction with non-native proteins as molecular chaperones. Here we analyzed the stability and oligomeric structure of murine Hsp25 and its correlation with function. Upon unfolding, the tertiary and quaternary structure of Hsp25 is rapidly lost, whereas the secondary… Expand
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