Mutation or deletion of the C-terminal tail affects the function and structure of Xenopus laevis small heat shock protein, hsp30.

@article{Fernando2002MutationOD,
  title={Mutation or deletion of the C-terminal tail affects the function and structure of Xenopus laevis small heat shock protein, hsp30.},
  author={Pasan Fernando and Rashid Abdulle and Ashvin Mohindra and J Guy Guillemette and John J. Heikkila},
  journal={Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
  year={2002},
  volume={133 1},
  pages={95-103}
}
Small heat shock proteins (shsps) act as molecular chaperones by preventing heat-induced aggregation and unfolding of cellular proteins by a mechanism that is still unclear. Previously we found that the C-terminal end of Xenopus shsp, hsp30C (30C), was essential for optimal chaperone activity. Examination of the C-terminal tail of 30C revealed that it had a net negative charge. Involvement of this negative charge in chaperone activity was assessed by the creation of two mutants, D209G (Asp… CONTINUE READING

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