title: The "π-Clamp" Offers a New Strategy for Site-Selective Protein Modification.
abstract: Pentelute and co-workers have identified a small encodable cysteine-containing peptide sequence that allows selective modification with perfluoroaryl probes. This π-clamp requires no external catalyst and is not limited to certain positions within a protein.
authors.affiliation: Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA.
authors.forename: Jeffery M
authors.initials: JM
authors.lastname: Tharp
authors.affiliation: Department of Chemistry, Texas A&M University, College Station, TX, 77843, USA. wliu@chem.tamu.edu.
authors.forename: Wenshe R
authors.initials: WR
authors.lastname: Liu
mesh_terms: D001710:Biotin / Q000737:chemistry / Q000378:metabolism; D002384:Catalysis; D003545:Cysteine / Q000378:metabolism; D005466:Fluorocarbons / Q000737:chemistry; D005982:Glutathione Transferase / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D005466:Fluorocarbons; D011506:Proteins; D001710:Biotin; C003005:hexafluorobenzene; D005982:Glutathione Transferase; D003545:Cysteine
keywords: cysteine; pi clamp; protein modification; site selectivity