Solid-State CI NMR Spectroscopy of Hydrochloride Salts of Amino Acids Implicated in Chloride Ion Transport Channel Selectivity: Opportunities at 900 MHz.
The results of a detailed systematic chlorine solid-state NMR study of several hydrochloride salts of amino acids implicated in chloride ion transport channel selectivity are reported. Cl and Cl NMR spectra have been obtained for stationary and/or magic-angle spinning powdered samples of the followi...
| Publicado en: | Journal of the American Chemical Society Vol. 128; no. 6; pp. 2121 - 2135 |
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| Autores principales: | , , |
| Formato: | Artículo |
| Publicado: |
American Chemical Society
2/15/2006
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| Materias: | |
| 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=20080050&site=ehost-live header: @attributes: shortDbName: hlh uiTerm: 20080050 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: 2/15/2006 vid: 128 iid: 6 pid: 997 pub: American Chemical Society artinfo: ui: 20080050 10.1021/ja057253i ppf: 2121 ppct: 14 formats: tig: atl: Solid-State CI NMR Spectroscopy of Hydrochloride Salts of Amino Acids Implicated in Chloride Ion Transport Channel Selectivity: Opportunities at 900 MHz. aug: au: Bryce, David L. Sward, Gregory D. Adiga, Samyuktha affil: Department of Chemistry, University of Ottawa, Ottawa, Ontario KIN 6N5, Canada. su: Nuclear magnetic resonance spectroscopy Amino acids Halogens Ion channels Spectrum analysis Optical diffraction Electronic structure sug: subj: Nuclear magnetic resonance spectroscopy Amino acids Halogens Ion channels Spectrum analysis Optical diffraction Electronic structure ab: The results of a detailed systematic chlorine solid-state NMR study of several hydrochloride salts of amino acids implicated in chloride ion transport channel selectivity are reported. Cl and Cl NMR spectra have been obtained for stationary and/or magic-angle spinning powdered samples of the following compounds on 500 and/or 900 MHz spectrometers: DL-arginine HCI monohydrate, L-lysine HCI, L-serine HCI, L-glutamic acid HCI, L-proline HCI, L-isoleucine HCI, L-valine HCI, L-phenylalanine HCI, and glycine HCI. Spectral analyses provide information on the anisotropic properties and relative orientations of the chlorine electric field gradient and chemical shift (CS) tensors, which are intimately related to the local molecular and electronic structure. Data obtained at 900 MHz provide unique examples of the effects of CS anisotropy on the NMR spectrum of a quadrupolar nucleus. The range of chlorine quadrupolar coupling constants (C) measured, -6.42 to 2.03 MHz, demonstrates the sensitivity of this parameter to the chloride ion environment and suggests the applicability of chlorine solid-state NMR as a novel experimental tool for defining chloride binding environments in larger ion channel systems. Salts of hydrophobic amino acids are observed to tend to exhibit larger values of C than salts of hydrophilic amino acids. A simple model for rationalizing the observed trend in C is proposed. For salts for which neutron diffraction structures are available, we identify a quantum chemical method which reproduces experimental values of C with a root-mean-square deviation of 0.1 MHz and a correlation coefficient of 0.9998. On the basis of this, chlorine NMR tensors are predicted for the Cl binding site in CIC channels. pubtype: Academic Journal doctype: Article src: R language: English refInfo: copyright: @attributes: flag: Y dt: @attributes: year: 2006 holdings: @attributes: islocal: N |
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