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231224s2013 xx |||||o 00| ||eng c |
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|a 10.1002/mrc.4007
|2 doi
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|a pubmed25n0769.xml
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|a (NLM)24038445
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|a DE-627
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|a eng
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|a Tugarinov, Vitali
|e verfasserin
|4 aut
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|a Four-bond deuterium isotope effects on the chemical shifts of amide nitrogens in proteins
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|c 2013
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 08.10.2015
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|a Date Revised 02.05.2015
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2013 John Wiley & Sons, Ltd.
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|a 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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|a Journal Article
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|a chemical shifts
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|a deuteration
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|a deuterium isotope shifts
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|a isotope filtering
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|a Amides
|2 NLM
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|a Protons
|2 NLM
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|a Ubiquitin
|2 NLM
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|a Deuterium
|2 NLM
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|a AR09D82C7G
|2 NLM
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|a Nitrogen
|2 NLM
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|a N762921K75
|2 NLM
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|i Enthalten in
|t Magnetic resonance in chemistry : MRC
|d 1985
|g 51(2013), 11 vom: 04. Nov., Seite 722-8
|w (DE-627)NLM098179667
|x 1097-458X
|7 nnns
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| 773 |
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|g volume:51
|g year:2013
|g number:11
|g day:04
|g month:11
|g pages:722-8
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|u http://dx.doi.org/10.1002/mrc.4007
|3 Volltext
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