Symmetry of the Surface, and Structure of the Central Core of Human LDL Particles, Analyzed by X-Ray Small Angle Scattering

  • M. W. Baumstark
  • W. Kreutz
  • A. Berg
  • J. Keul
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 285)


Although there exists a widely accepted model of the general structure of the LDL particle, there are still some important open questions, the most interesting being the three dimensional structure of the apoB molecule. There is very little knowledge of the exact conformation of this large polypeptide chain, containing many hydrophobic residues. Despite this hydrophobicity it was shown by several techniques (MABs, NMR, FTIR) that many domains of this protein are localized at the particle surface or are at least accessible to the solvent.


Acyl Chain Cholesterol Ester Radial Symmetry Electron Density Profile Symmetric Particle 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • M. W. Baumstark
    • 1
    • 2
  • W. Kreutz
    • 2
  • A. Berg
    • 1
  • J. Keul
    • 1
  1. 1.Med. UniversitätsklinikUniversität FreiburgFreiburgGermany
  2. 2.Inst. f. BiophysikUniversität FreiburgFreiburgGermany

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