title: Analysis of peptide secondary structures by photoactivatable amino acid analogues.
abstract: Photochemical cross-linking was applied to trap intramolecular interactions in peptides. The incorporation of diazirine-labeled amino acid analogues in combination with high-resolution mass spectrometry made it possible to catch reverse-turn conformations within peptides, exactly map their self-interacting surfaces, and discriminate between stable and transient interactions.
authors.affiliation: Pharmaceutical Chemistry and Bioanalytics, Martin-Luther-Universität Halle-Wittenberg, Institut für Pharmazie, Wolfgang-Langenbeck-Strasse 4, 06108 Halle, Germany. knut.koelbel@pharmazie.uni-halle.de
authors.forename: Knut
authors.initials: K
authors.lastname: Kölbel
authors.forename: Christian H
authors.initials: CH
authors.lastname: Ihling
authors.forename: Andrea
authors.initials: A
authors.lastname: Sinz
mesh_terms: D000345:Affinity Labels / Q000737:chemistry; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D021241:Spectrometry, Mass, Electrospray Ionization; D014466:Ultraviolet Rays
chemical_list: D000345:Affinity Labels; D000596:Amino Acids; D010455:Peptides