Literature DB >> 1807352

The hand of the helix of deoxyhemoglobin S fibers.

M R Lewis1, T E Lee, R Josephs.   

Abstract

Electron micrographs of deoxyhemoglobin S fiber cross sections provide an end-on view of the fiber whose appearance is sensitive to small changes in orientation. We have developed a procedure to exploit this sensitivity in order to determine the hand of these particles. In a sickle hemoglobin fiber the hemoglobin molecules form long pitch helical strands which twist about the particle axis with a pitch of about 3000 A. Tilting a 400-A-thick cross section by a few degrees aligns one of the long pitch helices so that it is nearly parallel to the direction of view. When a strand of hemoglobin molecules in a fiber is aligned in this manner it appears as a strongly contrasted bright spot. It is this spot, rather than the fiber axis, which appears to be the apparent center of rotation of the cross section. The direction of the displacement of the spot from the particle axis depends upon the particle hand and tilt direction. We have used this property to determine that sickle hemoglobin fibers are right-handed particles. This method may be applicable to other particles with long pitch helices as well.

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Year:  1991        PMID: 1807352     DOI: 10.1016/1047-8477(91)90022-o

Source DB:  PubMed          Journal:  J Struct Biol        ISSN: 1047-8477            Impact factor:   2.867


  1 in total

1.  Analysis of the stability of hemoglobin S double strands.

Authors:  X Q Mu; L Makowski; B Magdoff-Fairchild
Journal:  Biophys J       Date:  1998-01       Impact factor: 4.033

  1 in total

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