Peptide Secondary Structures in the Gas Phase: Consensus Motif of N-Linked Glycoproteins.
The possibility of secondary structure acting as a primary determinant in nature's choice of the consensus sequon, NXS/T in all N-linked glycoproteins, has been addressed by determining the intrinsic secondary structures of the capped oligopeptide, Ac-NGS-NHBn, and two "mutants", Ac-QGS-NHBn and Ac-...
| Publicado en: | Journal of the American Chemical Society Vol. 131; no. 3; pp. 1282 - 1288 |
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| Autores principales: | , , , , |
| Formato: | Artículo |
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American Chemical Society
1/28/2009
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=hlh&AN=36570865&site=ehost-live header: @attributes: shortDbName: hlh uiTerm: 36570865 longDbName: Humanities International Complete uiTag: AN controlInfo: bkinfo: jinfo: jid: 00027863 ACS jtl: Journal of the American Chemical Society issn: 00027863 maglogo: N pubinfo: dt: 1/28/2009 vid: 131 iid: 3 pid: 997 pub: American Chemical Society artinfo: ui: 36570865 10.1021/ja808687j ppf: 1282 ppct: 6 formats: tig: atl: Peptide Secondary Structures in the Gas Phase: Consensus Motif of N-Linked Glycoproteins. aug: au: Cocinero, Emilio J. Stanca-Kaposta, E. Cristina Gamblin, David P. Davis, Benjamin G. Simons, John P. affil: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, United Kingdom. Department of Chemistry, Chemical Research Laboratory, University of Oxford, Mansfield Road, Oxford OX1 4TA, United Kingdom. su: Chemical structure Glycoproteins Infrared spectroscopy Density functionals Dipole moments Glycosylation sug: subj: Chemical structure Glycoproteins Infrared spectroscopy Density functionals Dipole moments Glycosylation ab: The possibility of secondary structure acting as a primary determinant in nature's choice of the consensus sequon, NXS/T in all N-linked glycoproteins, has been addressed by determining the intrinsic secondary structures of the capped oligopeptide, Ac-NGS-NHBn, and two "mutants", Ac-QGS-NHBn and Ac-NPS-NHBn, by use of infrared laser ion dip spectroscopy in the gas phase coupled with ab initio and density functional theory calculation. Their global minimum energy conformations, exclusively or preferentially populated in all three peptides, display marked differences. NGS adopts an open, S-shaped backbone conformation rather than the C "Asx" turn structure that all previous measurements have identified in solution; the difference can be related to the high dipole moment of the "Asx" conformation and structural selection in a polar environment. QGS adopts a similar but more rigid backbone structure, supported by markedly stronger hydrogen bonds. NPS adopts an Asx turn coupled with a C β-turn backbone conformation, a structure also adopted in a crystal environment. These and other more subtle structural differences, particularly those involving interactions with the carboxamide side chain, provide strong evidence for the operation of structural constraints, and a potential insight into the unique reactivity of the asparagine side chain toward enzymatic glycosylation. pubtype: Academic Journal doctype: Article src: R language: English refInfo: copyright: @attributes: flag: Y dt: @attributes: year: 2009 holdings: @attributes: islocal: N |
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