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Related Experiment Videos

Linderstrom-Lang-Schellman's model for protein stabilization revisited.

Hiroshi Taniuchi1, Alan N Schechter, Joseph Shiloach

  • 1Laboratory of Chemical Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. htaniuch@helix.nih.gov

Current Protein & Peptide Science
|August 24, 2004
PubMed
Summary

Protein domains, stabilized by cooperative interactions, explain how cleaving one peptide bond alters protein structure. This cooperative interaction, involving a polarizable hydrophobic core, is key to protein stability and 3D domain swapping.

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Area of Science:

  • Protein structure and dynamics
  • Biophysics
  • Molecular biology

Background:

  • Cleavage of single peptide bonds in proteins can cause widespread conformational changes, even in distant regions.
  • The precise mechanisms underlying these extensive alterations remain incompletely understood.

Purpose of the Study:

  • To propose and support a model explaining how single peptide bond cleavage induces significant protein conformational changes.
  • To elucidate the role of cooperative interactions within protein structural domains in protein stability and 3D domain swapping.

Main Methods:

  • Review and analysis of existing experimental data on protein fragment complexation, folding, and stabilization.
  • Examination of protein structures, including 3D domain swapping and circular permutation.

Related Experiment Videos

  • Integration of models for electrostatic interactions and hydrophobic core properties.

    • Main Results:

    • Protein structural domains, stabilized by cooperative interactions, are central to the observed conformational changes upon peptide bond cleavage.
    • These cooperative interactions are crucial for protein stabilization and the determination of the native protein's ground state.
    • Domains typically possess a hydrophobic core that is polarizable and contributes to domain stabilization through interactions with surface charges.

    Conclusions:

    • Cooperative domain interactions are fundamental to protein stabilization and the mechanism of 3D domain swapping.
    • The polarizable hydrophobic core of protein domains plays a significant role in stabilizing these structures by responding to surface charges.
    • This model provides a partial explanation for the nature of cooperative interactions within protein domains.