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Structural conservation in globular proteins.

V N Viswanadhan, K Sundaram

    International Journal of Peptide and Protein Research
    |February 1, 1983
    PubMed
    Summary
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    Protein evolution shows conserved residues cluster together due to natural selection. Even non-conserved sites can form specific folding units, revealing evolutionary insights.

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Evolutionary Biology

    Background:

    • Understanding protein evolution relies on analyzing homologous protein sequences and their structures.
    • Conserved residues are key indicators of functional and structural importance.
    • Previous studies focused on individual conserved sites, but their spatial relationships are less explored.

    Purpose of the Study:

    • To investigate the nature of structural conservation in homologous proteins during evolution.
    • To identify patterns of residue association around conserved sites.
    • To explore the functional significance of non-conserved residues.

    Main Methods:

    • Analysis of well-sequenced homologous protein families.
    • Examination of representative tertiary protein structures.

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  • Application of an information theory approach to assess residue variability.

    • Main Results:

    • Conserved residue sites exhibit preferential association with other conserved sites within their 'sphere of influence', indicating natural selection.
    • This pattern of association is consistent across all residue types.
    • Non-conservative sites can also form clusters with high biochemical specificity and intermediate folding units.

    Conclusions:

    • Structural conservation in proteins is a complex process involving both individual site conservation and site clustering.
    • Natural selection actively shapes the spatial arrangement of residues around conserved sites.
    • Non-conserved residues can play critical roles in protein structure and function, contributing to folding units.