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Kinetic and equilibrium folding intermediates

O B Ptitsyn1, V E Bychkova, V N Uversky

  • 1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region.

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|April 29, 1995
PubMed
Summary

The molten globule state is a distinct thermodynamic state of proteins, separated by phase transitions. A novel pre-molten globule intermediate also exists, and protein denaturation occurs under specific pH and dielectric conditions.

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Area of Science:

  • Protein folding dynamics
  • Thermodynamics of biomolecules
  • Biophysical chemistry

Background:

  • Understanding protein folding intermediates is crucial for comprehending protein structure-function relationships.
  • The molten globule state is a key intermediate in protein folding pathways.
  • Existing models do not fully explain the thermodynamic properties and transitions of these states.

Purpose of the Study:

  • To elucidate the thermodynamic nature of the molten globule state.
  • To identify and characterize novel protein folding intermediates.
  • To investigate the conditions leading to protein denaturation and ligand release.

Main Methods:

  • Experimental investigation of protein folding intermediates.
  • Thermodynamic analysis of phase transitions.

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  • Characterization of protein denaturation under varying conditions.

    • Main Results:

    • The molten globule state is thermodynamically distinct, separated by intramolecular first-order phase transitions from native and unfolded states.
    • A novel equilibrium folding intermediate, the 'pre-molten globule' state, was identified, potentially analogous to kinetic intermediates.
    • Protein denaturation and non-polar ligand release were observed at moderately low pH and dielectric constants.

    Conclusions:

    • The molten globule represents a unique thermodynamic state in protein folding.
    • The pre-molten globule state offers new insights into folding pathways.
    • Denaturation conditions identified may be relevant to biological membranes.