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Limited cooperativity in protein folding.

Victor Muñoz1, Luis A Campos2, Mourad Sadqi3

  • 1National Biotechnology Center, Consejo Superior de Investigaciones Científicas, Darwin 3, Campus de Cantoblanco, 28049 Madrid, Spain; IMDEA Nanosciences, Faraday 9, Ciudad Universitaria Cantoblanco, 28049 Madrid, Spain; School of Engineering, University of California, 95343 Merced, CA, USA.

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Summary

Protein folding reactions exhibit limited structural cooperativity, impacting native state stability. This finding links folding speed to unfolding diversity, revealing a scale from pliable to disordered protein states.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Biophysics

Background:

  • Protein folding reactions are predicted to have low structural cooperativity.
  • Experimental studies of folding cooperativity have advanced significantly with new techniques.
  • Conformational ensembles are now preferred over discrete states for analysis.

Purpose of the Study:

  • To experimentally investigate the extent of structural cooperativity in protein folding.
  • To link the kinetics of protein folding and unfolding to the cooperativity of the process.
  • To establish a scale of protein cooperativity from two-state to intrinsically disordered proteins.

Main Methods:

  • Utilized advanced analytical procedures focusing on conformational ensembles.
  • Employed experimental techniques with enhanced time, structural, and single-molecule resolution.
  • Performed combined thermodynamic and kinetic analysis of fast protein folding.

Main Results:

  • Demonstrated a general scenario of limited cooperativity in protein folding.
  • Observed gradual structural disorder in both unfolded and native states, increasing with folding speed.
  • Established a direct correlation between protein folding/unfolding speed and equilibrium unfolding cooperativity.

Conclusions:

  • Limited cooperativity destabilizes native protein structures by affecting unfolding more than folding.
  • A continuous cooperativity scale can be defined, ranging from two-state folding to intrinsically disordered proteins.
  • Gradual unfolding and intrinsic disorder suggest a conformational rheostat mechanism for allosteric effects in folding-coupled binding.