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Self-assembly of biological macromolecules.

R N Perham

    Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
    |November 6, 1975
    PubMed
    Summary

    Cellular macromolecules like proteins self-assemble into complex structures. This process involves kinetically determined folding pathways and subunit aggregation, crucial for biological function and evolution.

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    Area of Science:

    • Biochemistry and Molecular Biology
    • Structural Biology
    • Biophysics

    Background:

    • The genetic apparatus directs macromolecule biosynthesis, leading to spontaneous folding and aggregation into biologically active tertiary and quaternary structures.
    • Self-assembly spans from simple monomers to complex multimeric structures, including those with multiple polypeptide chains and non-protein components.
    • Protein folding is a kinetically determined process, with folded proteins representing minimum free energy states within accessible conformations.

    Purpose of the Study:

    • To explore the principles governing the self-assembly of biological macromolecules.
    • To understand the role of folding pathways, subunit aggregation, and symmetry in forming complex biological structures.
    • To discuss the evolutionary advantages and functional implications of quaternary structure in proteins and viruses.

    Main Methods:

    • Analysis of existing evidence on protein folding and aggregation pathways.
    • Application of symmetry principles to model self-assembling structures.
    • Comparison of subunit compositions in various oligomeric enzymes and viral structures.
    • Discussion of nucleation events and stable intermediates in self-assembly.

    Main Results:

    • Denatured subunits of oligomeric enzymes likely adopt near-native structures before aggregation.
    • Symmetry arguments are effective for understanding structures with identical subunits, with allowances for quasi-equivalent bonding.
    • Protein stability increases with size, favoring subunit aggregation as an evolutionary strategy.
    • Quaternary structure confers biological advantages like cooperativity, altered specificity, and substrate channeling.

    Conclusions:

    • Self-assembly is a fundamental process in biology, driven by folding and aggregation guided by kinetic and thermodynamic principles.
    • Symmetry and quasi-symmetry play critical roles in the precise architecture of biological assemblies.
    • The evolution of quaternary structure enhances protein function and enables complex biological processes, as exemplified by enzymes and viruses.

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