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Related Experiment Videos

Volume changes on protein folding

Y Harpaz1, M Gerstein, C Chothia

  • 1Cambridge Centre for Protein Engineering, UK.

Structure (London, England : 1993)
|July 15, 1994
PubMed
Summary
This summary is machine-generated.

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High pressure alters protein folding by making the unfolded state more compact. New residue volume calculations reveal exceptionally high protein interior density, explaining this phenomenon and highlighting the role of packing forces in protein stability.

Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Science

Background:

  • Protein volume changes little during folding at low pressure.
  • At high pressure, the unfolded state is more compact than expected.
  • Molecular basis for this pressure-dependent behavior is unexplained.

Purpose of the Study:

  • To investigate the molecular origins of protein volume changes during folding.
  • To re-evaluate residue volumes within protein interiors.
  • To understand the contribution of packing density to protein stability.

Main Methods:

  • Redetermination of mean residue volumes in protein interiors.
  • Comparison of residue volumes in proteins versus solution.
  • Analysis of volume changes for different residue types (aliphatic, peptide, charged).

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Main Results:

  • New residue volumes indicate exceptionally high packing density in protein interiors.
  • Aliphatic groups occupy smaller volumes in proteins than in solution.
  • Peptide and charged groups occupy larger volumes in proteins than in solution.
  • Cancellation of these volume changes explains the small net volume change upon folding.

Conclusions:

  • The protein interior is exceptionally dense.
  • Packing forces play a significant role in protein stability.
  • This finding challenges previous assumptions about the dominant forces in protein folding.