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

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Zitation

Kleffel, B., Garavito, R. M., Baumeister, W., & Rosenbusch, J. P. (1985). Secondary structure of a channel-forming protein: porin from E. coli outer membranes. EMBO Journal., 4(6), 1589-1592.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-751C-6
Zusammenfassung
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.