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Related Experiment Videos

How fast is protein hydrophobic collapse?

Mourad Sadqi1, Lisa J Lapidus, Victor Muñoz

  • 1Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742, USA.

Proceedings of the National Academy of Sciences of the United States of America
|October 8, 2003
PubMed
Summary

Protein folding initiates with rapid hydrophobic collapse, occurring faster than secondary structure formation. This collapse dynamics slow at higher temperatures, revealing a dynamic hydrophobic effect.

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COCOMO2: A Coarse-Grained Model for Interacting Folded and Disordered Proteins.

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Area of Science:

  • Biophysics
  • Protein Dynamics
  • Chemical Physics

Background:

  • Understanding protein folding mechanisms is crucial for molecular biology.
  • The interplay between secondary structure formation and hydrophobic collapse remains a key question.
  • Isolating hydrophobic collapse from other folding events is experimentally challenging.

Purpose of the Study:

  • To directly measure the dynamics of protein hydrophobic collapse.
  • To investigate hydrophobic collapse in the absence of competing folding processes.
  • To explore the effect of temperature on hydrophobic collapse dynamics.

Main Methods:

  • Utilized laser-induced temperature jumps to trigger collapse in acid-denatured proteins.
  • Employed fluorescence resonance energy transfer (FRET) between probes at protein ends to monitor collapse.

Related Experiment Videos

  • Measured relaxation times of hydrophobic collapse at various temperatures.

    • Main Results:

    • Hydrophobic collapse occurs rapidly, with a relaxation time of approximately 60 ns at 305 K.
    • Collapse dynamics were found to be faster than secondary structure formation.
    • A slowdown in collapse dynamics was observed at higher temperatures, indicating a dynamic hydrophobic effect.

    Conclusions:

    • Proteins likely initiate folding via collapse into an unstructured globule under physiological conditions.
    • The observed dynamic hydrophobic effect is analogous to theoretical predictions of dynamic glass transitions.
    • Subsequent search for native structure is presumed to be driven by local motions within the collapsed globule.