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Related Experiment Videos

Autocatalyzed protein folding

S Veeraraghavan1, T F Holzman, B T Nall

  • 1Department of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78284-7760, USA.

Biochemistry
|August 20, 1996
PubMed
Summary
This summary is machine-generated.

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FKBP, a prolyl isomerase, catalyzes its own folding. This autocatalytic process speeds up slow folding phases involving proline isomerization, as demonstrated by FK506 inhibition.

Area of Science:

  • Biochemistry
  • Protein Folding
  • Enzymology

Background:

  • Proline isomerization is a slow step in protein folding.
  • Prolyl isomerases catalyze proline isomerization and often protein folding.
  • FKBP is a prolyl isomerase enzyme.

Purpose of the Study:

  • Investigate the folding kinetics of FKBP.
  • Determine if FKBP catalyzes its own folding.
  • Elucidate the role of proline isomerization in FKBP folding.

Main Methods:

  • Kinetic analysis of FKBP refolding.
  • Monitoring refolding in the presence and absence of native FKBP.
  • Assessing the effect of FK506, a prolyl isomerase inhibitor.

Main Results:

Related Experiment Videos

  • FKBP refolding exhibits three phases: fast (tau 3), intermediate (tau 2), and slow (tau 1).
  • Native FKBP accelerates the intermediate and slow folding phases, indicating proline isomerization involvement.
  • Autocatalytic folding of FKBP is observed, with the slow phase being concentration-dependent.
  • FK506 inhibits the autocatalysis of FKBP folding.

Conclusions:

  • The slow phase of FKBP folding is an autocatalyzed process.
  • Kinetically trapped species with non-native proline isomers are converted to native FKBP via autocatalysis.
  • FKBP folding serves as a model for autocatalysis in macromolecular conformational changes.