The oxidase DsbA folds a protein with a nonconsecutive disulfide.

@article{Messens2007TheOD,
  title={The oxidase DsbA folds a protein with a nonconsecutive disulfide.},
  author={Joris Messens and Jean-Francois Collet and Kinsley Belle and Elke Brosens and Remy Loris and Lode Wyns},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 43},
  pages={
          31302-7
        }
}
One of the last unsolved problems of molecular biology is how the sequential amino acid information leads to a functional protein. Correct disulfide formation within a protein is hereby essential. We present periplasmic ribonuclease I (RNase I) from Escherichia coli as a new endogenous substrate for the study of oxidative protein folding. One of its four disulfides is between nonconsecutive cysteines. In general view, the folding of proteins with nonconsecutive disulfides requires the protein… CONTINUE READING
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