title: Incorporation of an Unnatural Amino Acid as a Domain-Specific Fluorescence Probe in a Two-Domain Protein.
abstract: The biophysical analysis of multidomain proteins often is difficult because of overlapping signals from the individual domains. Previously, the fluorescent unnatural amino acid p-cyanophenylalanine has been used to study the folding of small single-domain proteins. Here we extend its use to a two-domain protein to selectively analyze the folding of a specific domain within a multidomain protein.
authors.affiliation: Laboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth , Universitätsstraße 30, D-95447 Bayreuth, Germany.
authors.forename: Lena K
authors.initials: LK
authors.lastname: Ries
authors.affiliation: Laboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth , Universitätsstraße 30, D-95447 Bayreuth, Germany.
authors.forename: Franz X
authors.initials: FX
authors.lastname: Schmid
authors.affiliation: Laboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth , Universitätsstraße 30, D-95447 Bayreuth, Germany.
authors.forename: Philipp A M
authors.initials: PA
authors.lastname: Schmidpeter
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D005456:Fluorescent Dyes / Q000737:chemistry*; D007700:Kinetics; D011506:Proteins / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
chemical_list: D000596:Amino Acids; D005456:Fluorescent Dyes; D011506:Proteins