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Photochemical labeling of membrane‐associated and channel‐forming domains of proteins directed by energy transfer
Author(s) -
Peng Ling,
Alcaraz Marie-Lyne,
Klotz Philippe,
Kotzyba-Hibert Florence,
Goeldner Maurice
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00392-0
Subject(s) - chemistry , chromophore , covalent bond , tryptophan , singlet state , energy transfer , membrane , ion channel , transmembrane protein , biophysics , ion , photochemistry , membrane protein , transmembrane domain , excited state , biochemistry , amino acid , chemical physics , organic chemistry , physics , receptor , biology , nuclear physics
Singlet—singlet energy transfer reactions from excited tryptophan residues to photoactivatable probes possessing a suitable chromophore, generate reactive species in the vicinity of the protein, leading to its covalent labeling. This delayed labeling process can be used to map the membrane‐surrounded regions of proteins with improved efficiency when it is applied with appropriate photoactivatable phospholipids. The same principle could also be applied to the labeling of channel‐forming transmembrane domains of ion channels, provided that suitable photoactivatable permeant ions were available. Both applications will be discussed with regard to their potential and feasibility.