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. 1986 Nov;5(11):3045–3049. doi: 10.1002/j.1460-2075.1986.tb04604.x

Localization of two chymotryptic fragments in the structure of renatured bacteriorhodopsin by neutron diffraction.

J Trewhella, J L Popot, G Zaccaï, D M Engelman
PMCID: PMC1167259  PMID: 3792306

Abstract

The structure of crystalline purple membrane reconstituted from purified bacteriorhodopsin (BR) chymotryptic fragments has been studied by neutron diffraction. In one of the samples studied, the fragment C-2, encompassing the first two predicted transmembrane segments, was prepared from deuterated purple membrane. The diffraction changes when the natural C-2 fragment is substituted by a deuterated one are analysed in terms of a seven-helix model for BR. The assignment of the labelled fragment to one end of the molecule placed new constraints on folding models for the protein.

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Selected References

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