title: Thioamide quenching of intrinsic protein fluorescence.
abstract: Thioamides quench tryptophan and tyrosine fluorescence in a distance-dependent manner and thus can be used to monitor the binding of thioamide-containing peptides to proteins. Since thioamide analogs of the natural amino acids can be synthetically incorporated into peptides, they can function as minimally-perturbing probes of protein/peptide interactions.
authors: Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, USA.
authors: Jacob M
authors: JM
authors: Goldberg
authors: Rebecca F
authors: RF
authors: Wissner
authors: Alyssa M
authors: AM
authors: Klein
authors: E James
authors: EJ
authors: Petersson
mesh_terms: D005453:Fluorescence; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D013854:Thioamides / Q000737:chemistry*; D014364:Tryptophan / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry
chemical_list: D010455:Peptides; D011506:Proteins; D013854:Thioamides; D014443:Tyrosine; D014364:Tryptophan