Your browser doesn't support javascript.
loading
Infrared multiple photon dissociation action spectroscopy of protonated glycine, histidine, lysine, and arginine complexed with 18-crown-6 ether.
McNary, Christopher P; Nei, Y-W; Maitre, Philippe; Rodgers, M T; Armentrout, P B.
Afiliación
  • McNary CP; Department of Chemistry, University of Utah, 315 S. 1400 E. Room 2020, Salt Lake City, Utah 84112, USA. armentrout@chem.utah.edu.
  • Nei YW; Department of Chemistry, Wayne State University, Detroit, Michigan 48202, USA. mrodgers@chem.wayne.edu.
  • Maitre P; Université Paris Sud, Laboratoire de Chimie Physique, UMR8000 CNRS, Faculté des Sciences, Bâtiment 350, 91405 Orsay Cedex, France.
  • Rodgers MT; Department of Chemistry, Wayne State University, Detroit, Michigan 48202, USA. mrodgers@chem.wayne.edu.
  • Armentrout PB; Department of Chemistry, University of Utah, 315 S. 1400 E. Room 2020, Salt Lake City, Utah 84112, USA. armentrout@chem.utah.edu.
Phys Chem Chem Phys ; 21(23): 12625-12639, 2019 Jun 21.
Article en En | MEDLINE | ID: mdl-31155616
Complexes of 18-crown-6 ether (18C6) with four protonated amino acids (AAs) are examined using infrared multiple photon dissociation (IRMPD) action spectroscopy utilizing light generated by the infrared free electron laser at the Centre Laser Infrarouge d'Orsay (CLIO). The AAs examined in this work include glycine (Gly) and the three basic AAs: histidine (His), lysine (Lys), and arginine (Arg). To identify the (AA)H+(18C6) conformations present in the experimental studies, the measured IRMPD spectra are compared to spectra calculated at the B3LYP/6-311+G(d,p) level of theory. Relative energies of various conformers and isomers are provided by single point energy calculations carried out at the B3LYP, B3P86, M06, and MP2(full) levels using the 6-311+G(2p,2d) basis set. The comparisons between the IRMPD and theoretical IR spectra indicate that 18C6 binds to Gly and His via the protonated backbone amino group, whereas protonated Lys prefers binding via the protonated side-chain amino group. Results for Arg are less definitive with strong evidence for binding to the protonated guanidino side chain (the calculated ground conformer at most levels of theory), but contributions from backbone binding to a zwitterionic structure are likely.

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Phys Chem Chem Phys Asunto de la revista: BIOFISICA / QUIMICA Año: 2019 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Phys Chem Chem Phys Asunto de la revista: BIOFISICA / QUIMICA Año: 2019 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido