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Aiding in folding: molecular chaperones and chaperonins

  • Engelbert Buxbaum

Abstract

C. Anfinsen could show that denatured (boiled or urea-treated) RNase could resume its correct folding once the temperature or urea concentration had been lowered [4]. He postulated that all proteins contain in their primary structure (amino acid sequence) the complete information which determines their secondary and tertiary structure (folding in 3-dimensional space). This hypothesis has proven fruitful (Nobel Price 1972).

Keywords

Molecular Chaperone Substrate Protein Protein Binding Site Yersinia Pestis Alexander Disease 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer 2007

Authors and Affiliations

  • Engelbert Buxbaum
    • 1
  1. 1.Department of BiochemistryRoss University School of MedicineWest Indies

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