Aiding in folding: molecular chaperones and chaperonins
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 . 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).
KeywordsMolecular Chaperone Substrate Protein Protein Binding Site Yersinia Pestis Alexander Disease
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