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Related Experiment Videos

Multiple intermediates and transition states during protein unfolding

F N Zaidi1, U Nath, J B Udgaonkar

  • 1National Centre for Biological Sciences, TIFR Centre, Bangalore, India.

Nature Structural Biology
|December 24, 1997
PubMed
Summary

This study reveals two distinct pathways for barstar protein unfolding, each with unique intermediate structures. Despite structural differences, the energy barriers for these unfolding pathways are remarkably similar.

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Area of Science:

  • Protein folding dynamics
  • Biophysical chemistry
  • Structural biology

Background:

  • Understanding protein unfolding mechanisms is crucial for comprehending protein misfolding diseases.
  • Barstar is a small, well-characterized protein often used as a model system.
  • Urea is a common denaturant used to study protein unfolding thermodynamics and kinetics.

Purpose of the Study:

  • To investigate the kinetic pathways of barstar unfolding induced by urea.
  • To identify and characterize the intermediate states involved in protein unfolding.
  • To compare the structural and energetic properties of competing unfolding pathways.

Main Methods:

  • Rapid kinetic studies using urea as a denaturant.
  • Analysis of protein unfolding intermediates.

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  • Characterization of transition states on competing pathways.

    • Main Results:

    • Demonstrated at least two distinct unfolding pathways for barstar.
    • Identified two intermediates: one with native-like secondary structure and a solvated core, the other with lost secondary structure but an intact core.
    • Observed significant structural divergence but energetic similarity between transition states of the two pathways.

    Conclusions:

    • Barstar unfolding proceeds through at least two competing kinetic pathways.
    • The identified intermediates possess distinct structural features, highlighting the complexity of protein unfolding.
    • Energetic landscapes of protein folding can be similar despite divergent structural pathways.