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Related Experiment Videos

Kinetic partitioning during protein folding yields multiple native states

J F Sinclair1, M M Ziegler, T O Baldwin

  • 1Center for Macromolecular Design, Texas A&M University, College Station 77843-2128, USA.

Nature Structural Biology
|May 1, 1994
PubMed
Summary

This study challenges the protein folding thermodynamic hypothesis. We found a protein with two stable, non-equilibrating native states, suggesting kinetic partitioning determines the final protein conformation.

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Area of Science:

  • Protein folding dynamics
  • Biophysical chemistry
  • Molecular biology

Background:

  • The thermodynamic hypothesis posits that the native protein state is the most stable conformation.
  • This implies the native state is in equilibrium with all other protein conformations.
  • This equilibrium is assumed to occur on biologically relevant timescales.

Purpose of the Study:

  • To investigate proteins that may deviate from the standard thermodynamic model of folding.
  • To explore the existence of multiple, non-equilibrating native states.
  • To understand the role of kinetics in determining protein conformation.

Main Methods:

  • Investigated a specific protein exhibiting unusual folding behavior.
  • Analyzed the conformational states and their interconversion rates.

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  • Compared in vitro refolding pathways with in vivo folding processes.

    • Main Results:

    • Identified a protein existing in two distinct, stable states, both potentially 'native'.
    • These two native states do not equilibrate on a biologically meaningful timescale.
    • The protein's active conformation resides in one of several energy minima.

    Conclusions:

    • The findings suggest that the traditional thermodynamic hypothesis may not universally apply to protein folding.
    • Kinetic partitioning between different folding pathways appears to dictate the final attained state.
    • This has significant implications for understanding protein structure and function in biological systems.