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Related Experiment Videos

Molecular interactions in protein crystals: solvent accessible surface and stability.

S A Islam1, D L Weaver

  • 1Biomolecular Modelling Laboratory, Imperial Cancer Research Fund Laboratories, London, England.

Proteins
|January 1, 1990
PubMed
Summary

Protein surface area correlates with molecular weight in crystals. Hydrophobic interactions stabilize proteins in both solution and crystalline states, explaining crystal formation.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Protein Crystallography

Background:

  • Protein folding and stability in biological systems are influenced by hydrophobic interactions.
  • Understanding protein behavior in crystalline environments is crucial for structural determination.

Purpose of the Study:

  • To investigate the relationship between accessible surface area and molecular weight for proteins in a crystalline state.
  • To determine how the transition from a free to a crystalline environment affects protein accessible surface area.
  • To elucidate the role of hydrophobic interactions in protein crystal stability.

Main Methods:

  • Analysis of accessible surface areas for 58 monomeric and dimeric proteins.
  • Comparison of accessible surface areas in crystalline versus free states.

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  • Correlation analysis between accessible surface area and molecular weight.

    • Main Results:

    • A simple relationship was identified between accessible surface area and molecular weight for proteins in crystals.
    • A well-defined loss of accessible surface area occurs when proteins transition from a free to a crystalline environment.
    • Hydrophobic interactions were found to be a significant factor in protein crystal stability.

    Conclusions:

    • Accessible surface area is a predictable characteristic of proteins based on molecular weight in crystalline forms.
    • The observed reduction in surface area upon crystallization highlights the importance of crystal packing forces.
    • Hydrophobic interactions play a dual role, contributing to both protein stability in vivo and crystal formation in vitro.