Four-bond deuterium isotope effects on the chemical shifts of amide nitrogens in proteins
Copyright © 2013 John Wiley & Sons, Ltd.
| Veröffentlicht in: | Magnetic resonance in chemistry : MRC. - 1985. - 51(2013), 11 vom: 04. Nov., Seite 722-8 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2013
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| Zugriff auf das übergeordnete Werk: | Magnetic resonance in chemistry : MRC |
| Schlagworte: | Journal Article chemical shifts deuteration deuterium isotope shifts isotope filtering Amides Protons Ubiquitin Deuterium AR09D82C7G mehr... |
| Zusammenfassung: | Copyright © 2013 John Wiley & Sons, Ltd. An approach towards precision NMR measurements of four-bond deuterium isotope effects on the chemical shifts of backbone amide nitrogen nuclei in proteins is described. Three types of four-bond (15) N deuterium isotope effects are distinguished depending on the site of proton-to-deuterium substitution: (4)ΔN(N(i-1)D), (4)ΔN(N(i+1)D) and (4)ΔN(Cβ,(i-1)D). All the three types of isotope shifts are quantified in the (partially) deuterated protein ubiquitin. The (4)ΔN(N(i+1)D) and (4)ΔN(C(β,i-1)D) effects are by far the largest in magnitude and vary between 16 and 75 ppb and -18 and 46 ppb, respectively. A semi-quantitative correlation between experimental (4)ΔN(N(i+1)D) and (4)ΔN(C(β,i-1)D) values and the distances between nitrogen nuclei and the sites of (1)H-to-D substitution is noted. The largest isotope shifts in both cases correspond to the shortest inter-nuclear distances |
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| Beschreibung: | Date Completed 08.10.2015 Date Revised 02.05.2015 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1097-458X |
| DOI: | 10.1002/mrc.4007 |