title: Excimer fluorescence in lens proteins labelled with N-(1-pyrene)maleimide.
abstract: Lens proteins labelled with the sulphydryl reagent, N-(1-pyrene)maleimide exhibit pyrene excimer fluorescence around 470 nm. This was found to be associated with both the beta- and gamma-crystallins but not the alpha-crystallins. Disappearance of the 470 nm peak on exposure to denaturants indicates it arose from an intramolecular excimer. This excimer fluorescence provides a new and sensitive tool for monitoring conformational changes in the beta- and gamma-crystallins.
authors.affiliation: Russell Grimwade School of Biochemistry, Melbourne University, Victoria, Australia.
authors.forename: T
authors.initials: T
authors.lastname: Putilina
authors.forename: R C
authors.initials: RC
authors.lastname: Augusteyn
mesh_terms: D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D003459:Crystallins / Q000378:metabolism*; D005453:Fluorescence; D008301:Maleimides / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
chemical_list: D003459:Crystallins; D008301:Maleimides; C003944:N-(3-pyrene)maleimide