PMID:10731430

Citation	Marsh, D (2000) Infrared dichroism of twisted beta-sheet barrels. The structure of E. coli outer membrane proteins. J. Mol. Biol. 297:803-8
Abstract	The infrared dichroic ratios of the amide bands from oriented beta-barrels yield an experimental value for the mean orientation, beta, of the beta-strands, relative to the barrel axis. For a barrel of n strands, this then gives the shear number, S, that characterizes the stagger of the beta-sheet. Combining values of beta and n specifies the barrel geometry by using the optimized model of Murzin, Lesk & Chothia for regular barrels. Application to published infrared data on the Escherichia coli outer membrane protein, OmpA yields S=9-10 (n=8), a barrel radius of 0.81(+/-0.01) nm, and an internal free volume of 0.031 nm(3) per residue, where the average twist of the beta-sheets is theta approximately 28 degrees, and their coiling angle is epsilon approximately 1 degrees. Hydrophobic matching of the 2.6 nm transmembrane stretch partly determines the shear number of the OmpA beta-barrel.
Links	PubMed Online version:10.1006/jmbi.2000.3557
Keywords	Amides/chemistry; Amides/metabolism; Amino Acid Sequence; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/metabolism; Escherichia coli/chemistry; Hydrogen Bonding; Mathematics; Models, Molecular; Molecular Sequence Data; Porins/chemistry; Porins/metabolism; Protein Structure, Secondary; Spectrophotometry, Infrared
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