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. 1986 Jun 1;236(2):389–395. doi: 10.1042/bj2360389

Identification of the sites in opsin modified by photoactivated azido[125I]iodobenzene.

M D Davison, J B Findlay
PMCID: PMC1146852  PMID: 2944512

Abstract

Opsin labelled with photoactivated 1-azido-4-[125I]iodobenzene was proteolysed in situ with Staphylococcus aureus V8 proteinase to yield two radioactive membrane-bound fragments. These were separated, cleaved with CNBr and the resultant peptides sequenced in order to locate the radiolabelled residues. In the whole molecule, there was clear evidence for modification of at least 20 sites, identified as derivatives of cysteine, tryptophan, tyrosine, histidine and lysine residues. The probe primary reacted, therefore, with nucleophilic substituents. The positions of the modified sites relative to the confines of the phospholipid bilayer were consistent with all other studies on the disposition of the polypeptide chain. The location of these sites substantiated an earlier suggestion that not all the transmembrane segments should be regarded as continuous regular alpha-helices.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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