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Related Experiment Videos

[Relation between the lysozyme hydration isotherm and molecule packing in the solid phase].

S G Gevorkian, V N Morozov

    Biofizika
    |November 1, 1983
    PubMed
    Summary

    This study introduces a precise micromethod for measuring mass changes in protein crystals. Lysozyme hydration is significantly influenced by molecular packing, impacting water uptake.

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    Acta naturae·2019

    Area of Science:

    • Biophysics
    • Materials Science

    Context:

    • Accurate measurement of mass changes in protein crystals is crucial for understanding hydration dynamics.
    • Glutaraldehyde treatment is a common method for protein crystal stabilization.

    Purpose:

    • To present a novel micromethod for measuring mass changes in glutaraldehyde-treated protein crystals.
    • To investigate the hydration properties of hen egg-white lysozyme across different crystal forms and amorphous films.

    Summary:

    • A cantilevered tungsten micro-needle system was developed for precise mass change measurements (0.1% accuracy) of protein crystals.
    • Absorption isotherms for water uptake were determined for triclinic, monoclinic, and tetragonal lysozyme crystals, as well as amorphous films.
    • Results indicate that lysozyme hydration is highly dependent on molecular packing, affecting water uptake at various relative humidities.

    Impact:

    • Provides a sensitive tool for studying protein crystal hydration and stability.
    • Offers insights into the relationship between molecular arrangement and water interaction in proteins.
    • Contributes to a better understanding of protein behavior in different physical states.

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