Abstract
BASIC pancreatic trypsin inhibitor (BPTI) is a protein of fifty-eight amino acid residues, which inhibits the serine proteinases trypsin, chymotrypsin, plasmin and kallikrein. The sequence has been fully elucidated1 (Fig. 1) and the three-dimensional structure has been determined to high resolution by X-ray crystallography2,3. In connection with studies on the partial synthesis of analogues of BPTI for the investigation of protein folding, we have examined in detail cleavage of the protein by cyanogen bromide4. We have found that the chain-cleaved product is unstable, and that on standing it is spontaneously transformed into an analogue of BPTI containing an intact chain of fifty-eight amino acid residues.
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DYCKES, D., CREIGHTON, T. & SHEPPARD, R. Spontaneous Re-formation of a Broken Peptide Chain. Nature 247, 202–204 (1974). https://doi.org/10.1038/247202a0
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DOI: https://doi.org/10.1038/247202a0
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