Spontaneous Re-formation of a Broken Peptide Chain

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 elucidated 1 (Fig. 1) and the three-dimensional structure has been determined to high resolution...

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Bibliographic Details
Published in:Nature (London) 1974-01, Vol.247 (5438), p.202-204
Main Authors: DYCKES, D. F., CREIGHTON, T., SHEPPARD, R. C.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Aprotinin
Carbon Radioisotopes
Chemical Phenomena
Chemistry
Chromatography, Ion Exchange
Cyanogen Bromide
Humanities and Social Sciences
Hydrolysis
letter
multidisciplinary
Oxidation-Reduction
Peptide Fragments
Protein Conformation
Protein Denaturation
Science
Science (multidisciplinary)
Serine
Tritium
Trypsin
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Summary: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 elucidated 1 (Fig. 1) and the three-dimensional structure has been determined to high resolution by X-ray crystallography 2,3 . 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 bromide 4 . 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.
ISSN:0028-0836
1476-4687
DOI:10.1038/247202a0