Tilt, twist, and coiling in β-barrel membrane proteins: Relation to infrared dichroism

Tibor Páli, Derek Marsh

Research output: Contribution to journalArticle

28 Citations (Scopus)


The x-ray coordinates of β-barrel transmembrane proteins from the porins superfamily and relatives are used to calculate the mean tilt of the β-strands and their mean local twist and coiling angles. The 13 proteins examined correspond to β-barrels with 8 to 22 strands, and shear numbers ranging from 8 to 24. The results are compared with predictions from the model of Murzin, Lesk, and Chothia for symmetrical regular barrels. Good agreement is found for the mean strand tilt, but the twist angles are smaller than those for open β-sheets and β-barrels with shorter strands. The model is reparameterised to account for the reduced twist characteristic of long-stranded transmembrane β-barrels. This produces predictions of both twist and coiling angles that are in agreement with the mean values obtained from the x-ray structures. With the optimized parameters, the model can then be used to determine twist and coiling angles of transmembrane β-barrels from measurements of the amide band infrared dichroism in oriented membranes. Satisfactory agreement is obtained for OmpF. The strand tilt obtained from the x-ray coordinates, or from the reparameterised model, can be combined with infrared dichroism measurements to obtain information on the orientation of the β-barrel assembly in the membrane.

Original languageEnglish
Pages (from-to)2789-2797
Number of pages9
JournalBiophysical journal
Issue number6
Publication statusPublished - Jun 2001

ASJC Scopus subject areas

  • Biophysics

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