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Related Experiment Videos

Flexibility and rigidity in protein crystals.

D M Blow

    Ciba Foundation Symposium
    |January 1, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Protein disorder, observed through crystallography, suggests a role in controlling protein function. Rigid conformations favor reactivity and specificity, while disorder may regulate biological processes.

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    Area of Science:

    • Structural biology
    • Biochemistry
    • Molecular biology

    Background:

    • Crystallographic studies reveal increasing evidence of disorder in protein structures.
    • Disordered regions are observed in key proteins like pancreatic serine proteinase zymogens and tyrosyl-tRNA synthetase.

    Purpose of the Study:

    • To explore the implications of protein polypeptide chain disorder.
    • To investigate the relationship between protein conformation, reactivity, specificity, and control functions.

    Main Methods:

    • Analysis of crystallographic data for protein structures.
    • Comparative study of protein examples exhibiting disorder.

    Main Results:

    • Observed disorder in specific regions of the main polypeptide chain for certain proteins.

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  • Examples include pancreatic serine proteinase zymogens and tyrosyl-tRNA synthetase.

    • Conclusions:

    • Rigid protein conformations are associated with enhanced reactivity and specificity.
    • Protein disorder may serve as a regulatory mechanism controlling protein activity and function.