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Protein structural classes in five complete genomes

D Frishman, H W Mewes

    Nature Structural Biology
    |August 1, 1997
    PubMed
    Summary
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    Predicted protein folding patterns in genomes deviate from known structures, yet the balance between membrane and globular proteins remains consistent. This finding impacts our understanding of protein evolution and function.

    Area of Science:

    • Structural biology
    • Genomics
    • Bioinformatics

    Background:

    • Understanding protein structure and distribution is crucial for deciphering biological functions.
    • Known protein structures exhibit specific tendencies in folding types.
    • Genomic data offers a vast resource for predicting protein distributions.

    Purpose of the Study:

    • To predict the distribution of globular protein folding types across five complete genomes.
    • To compare these predictions with observed tendencies in known protein structures.
    • To investigate the conservation of the ratio between membrane and globular proteins.

    Main Methods:

    • Bioinformatic analysis of complete genomes.
    • Prediction of protein folding types.

    Related Experiment Videos

  • Comparative analysis of predicted versus known protein structures.

    • Main Results:

    • The predicted distribution of globular proteins across folding types differs significantly from observed patterns in known structures.
    • A conserved ratio between the number of predicted membrane proteins and predicted globular proteins was identified across the studied genomes.

    Conclusions:

    • Genomic predictions suggest a different landscape of globular protein folding than currently observed.
    • The conserved ratio of membrane to globular proteins implies a fundamental constraint in proteome composition.