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Intermediate filaments in alpha-keratins.

R D Fraser, T P MacRae, D A Parry

    Proceedings of the National Academy of Sciences of the United States of America
    |March 1, 1986
    PubMed
    Summary
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    Researchers modeled the stabilizing interactions of alpha-keratin intermediate filaments (IF) using x-ray diffraction and ionic interaction data. This model applies to both hard and soft alpha-keratins found in hair, wool, and skin.

    Area of Science:

    • Structural biology
    • Biochemistry
    • Materials science

    Background:

    • X-ray diffraction studies revealed alpha-keratins' intermediate filaments (IF) possess a helical structure with a defined dislocation.
    • Previous research established the surface lattice and molecular association at lattice points for IF.

    Purpose of the Study:

    • To develop a model for the interaction patterns stabilizing the IF framework in hard alpha-keratins.
    • To investigate the applicability of this model to soft alpha-keratins from the stratum corneum.

    Main Methods:

    • Combined existing x-ray diffraction data on IF structure with new data on ionic interactions.
    • Analyzed coiled-coil rope segments of IF molecules to understand stabilizing forces.

    Main Results:

    Related Experiment Videos

    • A plausible model for the stabilizing interactions within hard alpha-keratin IF was proposed.
    • Similar interaction patterns are suggested for soft alpha-keratin IF from the stratum corneum.

    Conclusions:

    • The proposed model provides insight into the structural integrity of alpha-keratin intermediate filaments.
    • The findings suggest a conserved mechanism of stabilization across different types of alpha-keratins.