Fluorescence energy transfer between Cys-10 residues in F-actin filaments.
Fluorescence energy transfer was measured between Cys-10 residues in an F-actin filament using 5-[2-((iodoacetyl)amino)-ethyl]aminonaphthalene-1-sulphonic acid (1,5-IAEDANS) as a fluorescence energy donor and 4-dimethylaminophenylazophenyl-4'-maleimide (DABMI) as the acceptor. Both labels were covalently attached to Cys-10 residues in an F-actin filament. Taking the helical structure of the F-actin filament into consideration, the radial coordinate of Cys-10 was calculated to be 23 A. This corresponds to a distance between adjacent sites along the long pitch helix of 56.1 A and along the genetic helix of 53.3 A.
D000199:Actins / Q000378:metabolism*; D000818:Animals; D003545:Cysteine; D004735:Energy Transfer; D005033:Ethylmaleimide / Q000494:pharmacology; D005456:Fluorescent Dyes; D046911:Macromolecular Substances; D009132:Muscles / Q000378:metabolism; D009282:Naphthalenesulfonates; D011817:Rabbits; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D004124:p-Dimethylaminoazobenzene / Q000031:analogs & derivatives
D000199:Actins; D005456:Fluorescent Dyes; D046911:Macromolecular Substances; D009282:Naphthalenesulfonates; C006421:1,5-I-AEDANS; C049748:4-dimethylaminophenylazophenyl-4'-maleimide; D004124:p-Dimethylaminoazobenzene; D003545:Cysteine; D005033:Ethylmaleimide