Carbon-13 NMR studies of amino acids: Chemical shifts, protonation shifts, microscopic protonation behavior

Surprenant, Henry L.; Sarneski, Joseph E.; Key, Ronald R; Byrd, James T.; Reilley, Charles N.

doi:10.1016/0022-2364(80)90247-4

Cited by 31 publications

(57 citation statements)

References 23 publications

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“…This result indicated that only one type of low-molecular-weight saccharide moiety was present on the S-layer protein of C thernohydrosulfuncum S102-70. (10,38). P-D-Glucose was determined by HMBC-NMR to be the sugar at the reducing end of the glycan chain.…”

Section: Resultsmentioning

confidence: 99%

Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70

et al. 1992

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Section: Resultsmentioning

confidence: 99%

Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70

et al. 1992

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“…Protonation of either the amino or carboxylate group generally favors an upfield shift of the nearby carbons, with of the β-carbon usually experiencing larger up-field than the α-carbon [16-18]. The pKa values of glutamate carboxylates are 2.19 and 4.25 while the protonation constants for dicarboxylic acids without an amino group are typically pKa1 ∼ 3 and pKa2 ∼ 5 to 7 [17,18]. Consequently it was not surprising to find a small but adequate upfield shift of 2HG relative to glutamate with changing pH from 7 to 6.…”

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confidence: 99%

Conditions for 13C NMR detection of 2-hydroxyglutarate in tissue extracts from isocitrate dehydrogenase-mutated gliomas

Pichumani

Mashimo

Baek

et al. 2015

Analytical Biochemistry

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13C NMR spectroscopy of extracts from patient tumor samples provides rich information about metabolism. However, in IDH-mutant gliomas 13C labeling is obscured in glutamate and glutamine by the oncometabolite, 2-hydroxyglutaric acid (2HG), prompting development of a simple method to resolve the metabolites. J-coupled multiplets in 2HG were similar to glutamate and glutamine and could be clearly resolved at pH 6. A cryogenically-cooled 13C probe but not J-resolved heteronuclear single quantum coherence spectroscopy significantly improved detection of 2HG. These methods enable the monitoring of 13C-13C spin-spin couplings in 2HG expressing IDH mutant gliomas.

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“…Based on this amount of sugar, an average of four to five glycosylation sites per S-layer subunit was calculated. Since fraction GP III was obtained after pronase digestion and Bio-Gel P-4 chromatography (25), this material was subjected to reversed-phase HPLC ( (44).…”

Section: Resultsmentioning

confidence: 99%

Complete structure of the tyrosine-linked saccharide moiety from the surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70

Christian¹,

Schulz²,

Schuster-Kolbe³

et al. 1993

J Bacteriol

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In this study, we have extended and completed a previous investigation (P. Messner, R. Christian, J. Kolbe, G. Schulz, and U. B. Sleytr, J. Bacteriol. 174:2236Bacteriol. 174: -2240Bacteriol. 174: , 1992) in which we demonstrated for the first time in prokaryotic organisms the presence of a novel 0-glycosidic linkage via tyrosine. The surface layer glycoprotein of the eubacterium Clostridium thermohydrosufuricum S102-70 is arranged in a hexagonal lattice, with center-to-center spacings of approximately 16.3 nm. Molecular weight determination by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of both glycosylated and chemically deglycosylated surface layer glycoprotein showed values for the monomeric subunits of 94,000 and 87,500, respectively. Glycopeptide fractions obtained after exhaustive pronase digestion of purified, intact glycoprotein were isolated by reversed-phase liquid chromatography. One-and two-dimensional nuclear magnetic resonance studies, together with chemical analyses and plasma desorption time-of-flight mass spectrometry, were used to elucidate the structure of the hexasaccharide moiety linked by the novel 0-glycosidic linkage to tyrosine. The combined evidence suggests the following structure:

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Carbon-13 NMR studies of amino acids: Chemical shifts, protonation shifts, microscopic protonation behavior

Cited by 31 publications

References 23 publications

Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70

Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70

Conditions for 13C NMR detection of 2-hydroxyglutarate in tissue extracts from isocitrate dehydrogenase-mutated gliomas

Complete structure of the tyrosine-linked saccharide moiety from the surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70

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