Molecular Imaging of Purified Na+/K+-ATPase Molecules in Canine Kidney Membranes Using Atomic Force Microscopy

  • Jose K. Paul
  • Mehdi Ganjeizadeh
  • Huiying Yu
  • Mamoru Yamaguchi
  • Kunio Takeyasu


In order to ultimately elucidate the structure-function relationships of macromolecules, it is necessary to deduce detailed structural features by high resolution imaging in parallel to other techniques. In the case of membrane proteins this task has proven to be typically challenging due to limited availability of suitable specimen-preparation techniques and narrow applicability of conventional imaging techniques that require at least 2-dimensional crystals for high resolution. So far, a combination of electron microscopy (EM) and X-ray diffraction techniques, has been the most successful in the analysis of some of membrane proteins such as bacteriorhodopsin (7), nicotinic acetylcholine receptor (21) and Ca2+-ATPase (5). Atomic force microscopy (AFM) is emerging as a powerful tool for analyzing biological samples at molecular resolutions (3,6). Recent successful application of AFM to the channel structure of gap-junction molecules has proven the potential applicability of this technique to the structural (and, thereby, functional) analysis of membrane proteins in general (8).


Atomic Force Microscopy 44th Annual Symposium Ouabain Binding Molecular Resolution Conventional Imaging Technique 
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Copyright information

© Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt 1994

Authors and Affiliations

  • Jose K. Paul
    • 2
  • Mehdi Ganjeizadeh
    • 2
  • Huiying Yu
    • 2
  • Mamoru Yamaguchi
    • 1
  • Kunio Takeyasu
    • 2
  1. 1.Department of Veterinary Anatomy and Cell BiologyThe Ohio State UniversityColumbusUSA
  2. 2.Department of Med. Biochem. and Biotechnology CenterThe Ohio State UniversityColumbusUSA

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