title: Modulation of the peptide backbone conformation by the selenoxo photoswitch.
abstract: Photocontrol of the backbone conformation is a useful step forward in regulating the bioactivities of peptides and proteins by means of external signals. In the present work, the selenium analogue of a peptide bond was introduced into tetrapeptides to obtain surprisingly stable selenoxo peptides. Selenoxo peptide bonds allow for a marked increase of cis content in the photostationary state of peptide chains when irradiated with UV light near 290 nm. Slow thermal re-equilibration with rate constants between 9.9 x 10(-4) and 1.3 x 10(-5) s(-1) shows that the transient nonequilibrium conformations exist long enough to monitor the isomer specificity of biochemical reactions.
authors.affiliation: Max-Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, D-06120 Halle/Saale, Germany.
authors.forename: Yun
authors.initials: Y
authors.lastname: Huang
authors.forename: Günther
authors.initials: G
authors.lastname: Jahreis
authors.forename: Christian
authors.initials: C
authors.lastname: Lücke
authors.forename: Dirk
authors.initials: D
authors.lastname: Wildemann
authors.forename: Gunter
authors.initials: G
authors.lastname: Fischer
mesh_terms: D010455:Peptides / Q000737:chemistry*; D055668:Photochemical Processes; D011487:Protein Conformation; D018036:Selenium Compounds / Q000737:chemistry*
chemical_list: D010455:Peptides; D018036:Selenium Compounds