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Anal Biochem. 2005 Jul 15;342(2):271-9.

Dual-targeted labeling of proteins using cysteine and selenomethionine residues.

Author information

1
Department of Chemistry, University of Waterloo, Waterloo, Ont., Canada N2L 3G1.

Abstract

A new strategy for dual site-selective labeling of proteins that uses metabolically incorporated selenomethionine as a target for covalent modification by iodoacetamide derivatives, forming selenonium salts, is described. In the absence of free cysteine, labeling is specific and efficient. Dual-targeted labeling of a protein can be achieved with combinations of unique cysteine and methionine residues, if the cysteine is labeled first with a maleimide or another reagent that does not react with the selenomethionine. The method should be useful in biophysical applications such as fluorescence energy transfer.

PMID:
15950913
DOI:
10.1016/j.ab.2005.04.036
[Indexed for MEDLINE]

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