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Folding units in globular proteins

A M Lesk, G D Rose

    Proceedings of the National Academy of Sciences of the United States of America
    |July 1, 1981
    PubMed
    Summary
    This summary is machine-generated.

    This study introduces a method to identify structural units in globular proteins, revealing a hierarchy of folding pathways. This protein folding hierarchy supports a model of hierarchical condensation for protein assembly.

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    Area of Science:

    • Structural biology
    • Biophysics
    • Computational biology

    Background:

    • Proteins fold into complex three-dimensional structures.
    • Understanding protein folding pathways is crucial for molecular biology.

    Purpose of the Study:

    • To develop a method for identifying compact, contiguous-chain structural units in globular proteins.
    • To describe the hierarchical folding pathways of proteins based on these units.

    Main Methods:

    • Utilizing X-ray coordinates to identify structural units.
    • Analyzing the self-association of these units to map folding pathways.
    • Employing computational analysis to explore possible assembly routes.

    Main Results:

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  • Identified a structural hierarchy in proteins, from monomers to helices and strands.
  • Demonstrated that larger structural units are combinations of smaller ones.
  • Found multiple, yet computationally manageable, pathways for protein assembly.

    • Conclusions:

    • The hierarchical organization of structural units supports a model of folding by hierarchical condensation.
    • Protein folding may involve stepwise association of hydrophobic clusters.
    • This hierarchical model explains the formation of folding intermediates.