Studies on the Principles That Govern the Folding of Protein Chains
نویسنده
چکیده
The telegram that I received from the Swedish Royal Academy of Sciences specifically cites ". . . studies on ribonuclease, in particular the relationship between the amino acid sequence and the biologically active conformation...” The work that my colleagues and I have carried out on the nature of the process that controls the folding of polypeptide chains into the unique three-dimensional structures of proteins was, indeed, strongly influenced by observations on the ribonuclease molecule, Many others, including Anson and Mirsky (1) in the '30s and Lumry and Eyring (2) in the ‘50s, had observed and discussed the reversibility of denaturation of proteins. However, the true elegance of this consequence of natural selection was dramatized by the ribonuclease work, since the refolding of this molecule, after full denaturation by reductive cleavage of its four disulfide bonds (Figure 1), required that only one of the 105
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