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. 1985 Jun;4(6):1589–1592. doi: 10.1002/j.1460-2075.1985.tb03821.x

Secondary structure of a channel-forming protein: porin from E. coli outer membranes.

B Kleffel, R M Garavito, W Baumeister, J P Rosenbusch
PMCID: PMC554386  PMID: 2992934

Abstract

Porin from Escherichia coli outer membranes has been analysed by high angle diffuse X-ray diffraction, and by attenuated total reflection infrared spectroscopy. These methods demonstrate independently that the majority of the polypeptide backbone is arranged in anti-parallel beta-pleated sheet structure. The average length of the beta-strands, which are oriented nearly normal to the membrane plane, is estimated to be 10-12 residues, independent of the method used. Although the details of strand arrangement (beta-barrels or stacked sheets) are not as yet known, porin represents the first transmembrane protein for which beta-structure has been established unequivocally.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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