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. 1990 Jul;87(13):5208–5212. doi: 10.1073/pnas.87.13.5208

On the structure of erythrocyte spectrin in partially expanded membrane skeletons.

A M McGough 1, R Josephs 1
PMCID: PMC54291  PMID: 2367532

Abstract

Spectrin is generally believed to play an important role in the erythrocyte membrane's ability to deform elastically. We have studied the structure of negatively stained spectrin in partially expanded membrane skeletons to determine how its molecular structure confers elastic properties on the cell membrane. Fourier analysis of electron micrographs of spectrin reveals that the alpha and beta subunits are twisted about a common axis, forming a two-start helix with twofold rotational symmetry. We propose that elastic deformation of the cell is mediated by transient extension of the helix by mechanical forces.

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