Affinity chromatography of GroEL chaperonin based on denatured proteins: Role of electrostatic interactions in regulation of GroEL affinity for protein substrates

@article{Marchenko2006AffinityCO,
  title={Affinity chromatography of GroEL chaperonin based on denatured proteins: Role of electrostatic interactions in regulation of GroEL affinity for protein substrates},
  author={Natasha Marchenko and Victor V. Marchenkov and Anna L Kaysheva and Ivan A. Kashparov and Natalia V. Kotova and Pavel A Kaliman and Gennady V. Semisotnov},
  journal={Biochemistry (Moscow)},
  year={2006},
  volume={71},
  pages={1357-1364}
}
The chaperonin GroEL of the heat shock protein family from Escherichia coli cells can bind various polypeptides lacking rigid tertiary structure and thus prevent their nonspecific association and provide for acquisition of native conformation. In the present work we studied the interaction of GroEL with six denatured proteins (α-lactalbumin, ribonuclease A, egg lysozyme in the presence of dithiothreitol, pepsin, β-casein, and apocytochrome c) possessing negative or positive total charge at… CONTINUE READING

References

Publications referenced by this paper.
Showing 1-2 of 2 references

Fundamentals of Fluorescent Spectroscopy [Russian translation], Mir, Moscow

  • J. Lakovich
  • 1986
1 Excerpt

Chromatography of Proteins and Nucleic Acids [in Russian], Nauka, Moscow

  • L. A. Osterman
  • 1985
1 Excerpt

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