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Related Experiment Videos

pH-dependent conformational changes of concanavalin A.

R Zand, B B Agrawal, I J Goldstein

    Proceedings of the National Academy of Sciences of the United States of America
    |September 1, 1971
    PubMed
    Summary

    Concanavalin A primarily adopts a beta conformation at acidic to neutral pH. At alkaline pH, it transitions to a random coil, with no significant alpha helix observed.

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    Histochemistry and cell biology·2001

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Spectroscopy

    Background:

    • Concanavalin A is a legume lectin with known biological activities.
    • Understanding protein conformation is crucial for elucidating function.
    • pH is a known factor influencing protein structure.

    Purpose of the Study:

    • To investigate the pH-dependent conformational changes of concanavalin A.
    • To correlate structural changes with functional activity.

    Main Methods:

    • Optical rotatory dispersion (ORD) spectroscopy.
    • Circular dichroism (CD) spectroscopy.

    Main Results:

    • Concanavalin A predominantly exhibits beta-conformation at pH 2.9, 5.0, and 7.0.
    • At pH 9.1, concanavalin A adopts a random coil or unordered structure.
    • No significant alpha-helical structure was detected across the studied pH range.
    • The pH dependence of the Moffitt equation parameter b(0) correlates with maximum precipitin-like activity.

    Conclusions:

    • Concanavalin A undergoes significant conformational changes with varying pH.
    • The beta-conformation is favored under acidic to neutral conditions.
    • Alkaline pH induces a loss of ordered structure, leading to a random coil.
    • Structural transitions are linked to the protein's biological activity.

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