Display Settings:

Format

Send to:

Choose Destination
    Science. 1991 Sep 20;253(5026):1386-93.

    Reexamination of the folding of BPTI: predominance of native intermediates.

    Source

    Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Cambridge, MA 02142.

    Abstract

    Bovine pancreatic trypsin inhibitor (BPTI) continues to be the only protein for which a detailed pathway of folding has been described. Previous studies led to the conclusion that nonnative states are well populated in the oxidative folding of BPTI. This conclusion has broadly influenced efforts to understand protein folding. The population of intermediates present during the folding of BPTI has been reexamined by modern separation techniques. It was found that all well-populated folding intermediates contain only native disulfide bonds. These data emphasize the importance of native protein structure for understanding protein folding.

    PMID:
    1716783
    [PubMed - indexed for MEDLINE]

      Supplemental Content

      Icon for HighWire Press

      Save items

      loading

      Recent activity

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      Write to the Help Desk