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Related Experiment Videos

Kinetic study on myoglobin refolding monitored by five optical probe stopped-flow methods

K Chiba1, A Ikai, Y Kawamura-Konishi

  • 1Laboratory of Biodynamics, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Kanagawa, Japan.

Proteins
|June 1, 1994
PubMed
Summary

Horse cyanometmyoglobin refolding occurs in three distinct phases, with rapid secondary and tertiary structure formation, including a heme pocket precursor, within milliseconds. These findings reveal key steps in myoglobin

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Area of Science:

  • Biophysics
  • Protein Folding
  • Spectroscopy

Background:

  • Myoglobin's refolding is crucial for its function.
  • Understanding protein folding kinetics aids in comprehending biological processes.

Purpose of the Study:

  • To investigate the refolding kinetics of horse cyanometmyoglobin.
  • To elucidate the structural changes during refolding using multiple optical probes.

Main Methods:

  • Stopped-flow spectroscopy utilizing absorption and circular dichroism (CD).
  • Monitoring changes at specific wavelengths (422 nm, 340 nm, 222 nm, 260 nm).
  • Investigating urea-induced refolding kinetics.

Main Results:

  • Three distinct refolding phases were identified with varying rate constants.

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  • Rapid formation of secondary structure (~40%) and a heme pocket precursor occurred within 10.7 ms.
  • Middle and slow phases involved tertiary structure formation and ligand exchange at the heme iron.

    • Conclusions:

    • A multi-phase model for myoglobin refolding, including heme group involvement, is proposed.
    • The rapid formation of structural elements is critical for functional recovery.
    • Kinetic intermediates play a significant role in the overall folding pathway.