title: Selective incorporation of nitrile-based infrared probes into proteins via cysteine alkylation.
abstract: The nitrile stretching vibration is increasingly used as a sensitive infrared probe of local protein environments. However, site-specific incorporation of a nitrile moiety into proteins is difficult. Here we show that various aromatic nitriles can be easily incorporated into peptides and proteins via either thiol alkylation or arylation reaction.
authors.affiliation: Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia,Pennsylvania 19104, United States.
authors.forename: Hyunil
authors.initials: H
authors.lastname: Jo
authors.forename: Robert M
authors.initials: RM
authors.lastname: Culik
authors.forename: Ivan V
authors.initials: IV
authors.lastname: Korendovych
authors.forename: William F
authors.initials: WF
authors.lastname: Degrado
authors.forename: Feng
authors.initials: F
authors.lastname: Gai
mesh_terms: D000478:Alkylation; D002147:Calmodulin / Q000737:chemistry* / Q000378:metabolism; D003545:Cysteine / Q000737:chemistry* / Q000378:metabolism; D005456:Fluorescent Dyes / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D009570:Nitriles / Q000737:chemistry* / Q000378:metabolism; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D013055:Spectrophotometry, Infrared / Q000379:methods; D014732:Vibration
chemical_list: C082965:CALML3 protein, human; D002147:Calmodulin; D005456:Fluorescent Dyes; D009570:Nitriles; D011506:Proteins; D003545:Cysteine