Isotope effects on chemical shifts of proteins and peptides

Hansen, Poul Erik

doi:10.1002/(sici)1097-458x(200001)38:1<1::aid-mrc594>3.0.co;2-4

Cited by 46 publications

(21 citation statements)

References 104 publications

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“…As in the case of the glucosamine analogs, two 15 anomers, respectively as a result of deuterium substitution. This solvent-dependent difference in nitrogen chemical shifts has been reported previously following exchange of nitrogen-bound protons with 2 H in protein amide groups [30,31]. Based on the pattern of long-range couplings observed in Fig.…”

Section: Fig 2 Shows the Results Obtained For The Pulse Sequences Ilsupporting

confidence: 86%

Getting to know the nitrogen next door: HNMBC measurements of amino sugars

Limtiaco

Langeslay

Béni

et al. 2011

Journal of Magnetic Resonance

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Section: Fig 2 Shows the Results Obtained For The Pulse Sequences Ilsupporting

confidence: 86%

Getting to know the nitrogen next door: HNMBC measurements of amino sugars

Limtiaco

Langeslay

Béni

et al. 2011

Journal of Magnetic Resonance

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“…The data were fit by y = x + b , with parameter b accounting for a small chemical shift reference difference in the two studies and isotope shift effects arose from use of a deuterated sample in the current study (Hansen 2000). The b value along with coefficient of determination R 2 are written in each sub-figure.…”

Section: Figmentioning

confidence: 99%

Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy

et al. 2012

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Solid-state NMR has emerged as an important tool for structural biology and chemistry, capable of solving atomic-resolution structures for proteins in membrane-bound and aggregated states. Proton detection methods have been recently realized under fast magic-angle spinning conditions, providing large sensitivity enhancements for efficient examination of uniformly labeled proteins. The first and often most challenging step of protein structure determination by NMR is the site-specific resonance assignment. Here we demonstrate resonance assignments based on high-sensitivity proton-detected three-dimensional experiments for samples of different physical states, including a fully-protonated small protein (GB1, 6 kDa), a deuterated microcrystalline protein (DsbA, 21 kDa), a membrane protein (DsbB, 20 kDa) prepared in a lipid environment, and the extended core of a fibrillar protein (α-synuclein, 14 kDa). In our implementation of these experiments, including CONH, CO(CA)NH, CANH, CA(CO)NH, CBCANH, and CBCA(CO)NH, dipolar-based polarization transfer methods have been chosen for optimal efficiency for relatively high protonation levels (full protonation or 100 % amide proton), fast magic-angle spinning conditions (40 kHz) and moderate proton decoupling power levels. Each H–N pair correlates exclusively to either intra- or inter-residue carbons, but not both, to maximize spectral resolution. Experiment time can be reduced by at least a factor of 10 by using proton detection in comparison to carbon detection. These high-sensitivity experiments are especially important for membrane proteins, which often have rather low expression yield. Proton-detection based experiments are expected to play an important role in accelerating protein structure elucidation by solid-state NMR with the improved sensitivity and resolution.

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“…57). Such a dependence is not restricted to glycine, and can be expected for all a-carbons as the C -H bond is hyperconjugated to the CONH group [27].…”

Section: Proteinsmentioning

confidence: 91%

“…Some new results in this field have been obtained [21 -26]. For simple aliphatic compounds a correlation between 13 C chemical shifts and one-bond isotope effects was shown, and was suggested to be suitable for prediction of the 1 DCðDÞ from dC-b in peptides and proteins [27]. The linear correlation between the chemical shift and 1 DCðDÞ was also found in a series of 3-substituted pyridines [23].…”

Section: One-bond Isotope Effects 1 Dcðdþmentioning

confidence: 99%