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Related Experiment Videos

Fast chain contraction during protein folding: "foldability" and collapse dynamics.

Linlin Qiu1, Cherian Zachariah, Stephen J Hagen

  • 1University of Florida, Physics Department, P.O. Box 118440, Gainesville, Florida 32611-8440, USA.

Physical Review Letters
|May 7, 2003
PubMed
Summary

Even disordered protein chains contract over an energetic barrier, similar to fast-folding proteins. This suggests that the protein

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Area of Science:

  • Protein dynamics
  • Biophysics
  • Molecular folding

Background:

  • Protein folding theories predict rapid, unimpeded collapse.
  • Experimental data show organized, barrier-limited collapse even in fast-folding proteins.
  • The role of kinetic barriers in protein collapse dynamics is unclear.

Purpose of the Study:

  • To investigate if kinetic barriers during collapse are linked to equilibrium foldability.
  • To measure chain contraction rates in nonfolding protein analogs.
  • To compare collapse dynamics of disordered chains with fast-folding proteins.

Main Methods:

  • Synthesized two nonfolding analogs of a fast-collapsing protein.
  • Measured the rate of chain contraction for these analogs.

Related Experiment Videos

  • Compared contraction timescales and energy barriers with the natural protein.

    • Main Results:

    • Nonfolding analogs contracted on a similar timescale (approximately 10^-5 s) as the natural protein.
    • Disordered chains encountered energetic barriers comparable to the folding protein.
    • Chain contraction was ~1000x slower than predicted for an ideal chain.

    Conclusions:

    • Equilibrium foldability does not solely dictate collapse dynamics.
    • Energetic barriers are present even in the collapse of disordered protein chains.
    • The dynamics of protein collapse are more complex than simple unimpeded chain contraction.