Aiding in folding: molecular chaperones and chaperonins

  • Engelbert Buxbaum


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).


Molecular Chaperone Substrate Protein Protein Binding Site Yersinia Pestis Alexander Disease 
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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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