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Related Experiment Videos

Intermediate filament structure: hard alpha-keratin

L N Jones1, M Simon, N R Watts

  • 1CSIRO Division of Wool Technology, Belmont, Vic., Australia.

Biophysical Chemistry
|February 20, 1998
PubMed
Summary
This summary is machine-generated.

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Hard alpha-keratin intermediate filaments (IF) have approximately 30 chains per cross-section. This structure, stabilized by disulfide bonds, aligns with other IF types, suggesting common aggregation principles.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Intermediate filaments (IFs) are a class of cytoskeletal proteins.
  • Four structural classes of IFs exist with related axial organizations.
  • Hard alpha-keratin IFs exhibit unique features requiring clarification.

Purpose of the Study:

  • To determine the number of molecules in the cross-section of hard alpha-keratin IFs.
  • To understand the stabilization mechanisms of hard alpha-keratin IF axial organization.
  • To compare hard alpha-keratin IF structure with other IF classes.

Main Methods:

  • Scanning Transmission Electron Microscopy (STEM) dark-field mode for mass measurements.
  • Analysis of unstained IF isolated from hair keratin.

Related Experiment Videos

  • Re-analysis of low-angle equatorial X-ray diffraction patterns.

    • Main Results:

    • STEM mass measurements indicate approximately 30 (+/-3) chains per cross-section for hard alpha-keratin IFs.
    • This number is consistent with previous STEM findings for other IF types (around 32 chains).
    • X-ray diffraction data supports the STEM-derived chain number, contrasting with earlier interpretations.

    Conclusions:

    • Native IFs, including hard alpha-keratin, desmin/vimentin, and likely others, contain about 32 chains in cross-section.
    • Hard alpha-keratin IFs may compensate for the lack of head-to-tail overlap with intermolecular disulfide bonds.
    • While axial structures vary, IFs generally follow similar basic aggregation modes.