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.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Marsh Ddoi
10.1006/jmbi.2000.3557keywords:
subject
Has Abstractpub_date
2000-03-31 00:00:00pages
803-8issue
3eissn
0022-2836issn
1089-8638pii
S0022-2836(00)93557-5journal_volume
297pub_type
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