Reductive cleavage of disulfide bridges in ribonuclease.

@article{Sela1957ReductiveCO,
  title={Reductive cleavage of disulfide bridges in ribonuclease.},
  author={M. Sela and F. H. White and C. Anfinsen},
  journal={Science},
  year={1957},
  volume={125 3250},
  pages={
          691-2
        }
}
This article was the first of many studies that were generally concerned with the eventual total synthesis of the protein. It contained several original observations that would lead to the conclusion that the refolding of the ribonuclease molecule after full denaturation by reductive cleavage of its four disulfide bonds required that only one of the one hundred five possible pairings of eight sulfhydryl groups to form four disulfide linkages take place. 
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Topics from this paper

SOME RELATIONSHIPS OF STRUCTURE TO FUNCTION IN RIBONUCLEASE
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IMMUNOCHEMICAL REACTIONS INVOLVING RIBONUCLEASE *
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Protection of Thiols
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Cleavage of one specific disulfide bond in papain.
  • 61
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The correlation of ribonuclease activity with specific aspects of tertiary structure.
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THE RELATION OF STRUCTURE TO ENZYMATIC ACTIVITY IN RIBONUCLEASE *
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The reformation of disulfide bridges in proteins.
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