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Related Experiment Videos

Protein folding intermediates: native-state hydrogen exchange

Y Bai1, T R Sosnick, L Mayne

  • 1Johnson Research Foundation, Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia 19104-6059, USA.

Science (New York, N.Y.)
|July 14, 1995
PubMed
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Cytochrome c unfolds through distinct intermediate states, revealing cooperative structural units. These findings illuminate the dynamic folding pathways of proteins even under native conditions.

Area of Science:

  • Biochemistry
  • Protein Dynamics
  • Structural Biology

Background:

  • Cytochrome c is a crucial protein involved in cellular respiration.
  • Understanding protein folding pathways is essential for comprehending biological function and disease.
  • Metastable states in protein unfolding offer insights into dynamic structural transitions.

Purpose of the Study:

  • To investigate the hydrogen exchange behavior of native cytochrome c.
  • To identify and characterize intermediate partially unfolded forms.
  • To elucidate the cooperative units and major pathways in cytochrome c folding.

Main Methods:

  • Hydrogen exchange analysis of native cytochrome c.
  • Characterization of protein structural dynamics.

Related Experiment Videos

  • Thermodynamic analysis of unfolding intermediates.

    • Main Results:

    • Low denaturant concentrations revealed a sequence of metastable, partially unfolded cytochrome c forms.
    • Unfolding occurs through the disruption of cooperative structural units (omega loops, helix-loop pairs).
    • Partially unfolded forms represent major intermediates in reversible unfolding reactions.

    Conclusions:

    • The identified intermediate forms define the major pathway for cytochrome c folding.
    • Cooperative structural units are key to the stepwise unfolding process.
    • Dynamic unfolding and refolding occur even at native protein conditions.