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Related Experiment Videos

Forcing thermodynamically unfolded proteins to fold

I Baskakov1, D W Bolen

  • 1Department of Human Biological Chemistry and Genetics, Sealy Center for Structural Biology, University of Texas Medical Branch, Galveston, Texas 77555-1052, USA.

The Journal of Biological Chemistry
|March 28, 1998
PubMed
Summary

Trimethylamine N-oxide (TMAO) can induce folding in disordered proteins, enhancing their stability and function. This osmolyte significantly increases the native state population, enabling structural and functional studies of these proteins.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Many biologically significant proteins are intrinsically disordered or partially unfolded.
  • Organisms utilize organic osmolytes to stabilize proteins against environmental stresses.

Purpose of the Study:

  • To investigate the capacity of trimethylamine N-oxide (TMAO) to induce folding in thermodynamically unfolded proteins.
  • To explore the potential of TMAO for structural and functional characterization of disordered proteins.

Main Methods:

  • Utilized TMAO as an osmolyte to treat two thermodynamically unfolded proteins.
  • Assessed protein folding, stability, and functional activity in the presence of TMAO.

Main Results:

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  • TMAO successfully induced native-like folding in both studied proteins.
  • One protein exhibited a nearly five-orders-of-magnitude increase in native state population due to TMAO.
  • Folded proteins displayed significant functional activity.

    • Conclusions:

    • TMAO demonstrates a remarkable ability to stabilize and induce functional structure in disordered proteins.
    • TMAO facilitates the study of intrinsically disordered proteins by promoting their folded state.
    • This finding opens avenues for structural and functional investigations of proteins that lack inherent structure.