beta barrel

A protein structural motif consisting of antiparallel beta strands that form a hydrophobic protein core with a large beta-sheet that twists and coils, resulting in a closed structure in which the first strand is hydrogen bonded to the last. Beta barrels are found in porins and transmembrane proteins and encoded by up to 3% of gram-negative bacterial genes.

Mentioned in

lipocalin

References in periodicals archive

In addition, X-ray data show that the chromophore responsible for the fluorescence lies within the beta barrel and is tilted approximately 60 degrees to the long axis of the barrel.

Fluorescence polarization of gfp crystals

Erickson, in collaboration with Jane and David Richardson of Duke University in Durham, N.C., devised a sequence of amino acids that comprises a structure far more regular than any "beta barrels" seen in nature.

Beyond the limits of protein building

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