Related ArticlesLow resolution (1)H NMR assignment of proton populations in pound cake and its polymeric ingredients.
Food Chem. 2013 Aug 15;139(1-4):120-8
Authors: Luyts A, Wilderjans E, Waterschoot J, Van Haesendonck I, Brijs K, Courtin CM, Hills B, Delcour JA
Abstract
Based on a model system approach, five different proton populations were distinguished in pound cake crumb using one dimensional low resolution (1)H NMR spectroscopy. In free induction decay (FID) measurements, proton populations were assigned to (i) non-exchanging CH protons of crystalline starch, proteins and crystalline fat and (ii) non-exchanging CH protons of amorphous starch and gluten, which are in little contact with water. In Carr-Purcell-Meiboom-Gill (CPMG) measurements, three proton populations were distinguished. The CPMG population with the lowest mobility and the FID population with the highest mobility represent the same proton population. The two CPMG proton populations with the highest mobility were assigned to exchanging protons (i.e., protons of water, starch, gluten, egg proteins and sugar) and protons of lipids (i.e., protons of egg yolk lipids and amorphous lipid fraction of margarine) respectively. Based on their spin-lattice relaxation times (T1), two dimensional (1)H NMR spectroscopy further resolved the two proton populations with the highest mobility into three and two proton populations, respectively.
Database proton NMR chemical shifts for RNA signal assignment and validation
Database proton NMR chemical shifts for RNA signal assignment and validation
Abstract The Biological Magnetic Resonance Data Bank contains NMR chemical shift depositions for 132 RNAs and RNA-containing complexes. We have analyzed the 1H NMR chemical shifts reported for non-exchangeable protons of residues that reside within A-form helical regions of these RNAs. The analysis focused on the central base pair within a stretch of three adjacent base pairs (BP triplets), and included both Watsonâ??Crick (WC; G:C, A:U) and G:U wobble pairs. Chemical shift values were included for all 43...
Towards automatic metabolomic profiling of high-resolution one-dimensional proton NMR spectra
Towards automatic metabolomic profiling of high-resolution one-dimensional proton NMR spectra
Abstract Nuclear magnetic resonance (NMR) and Mass Spectroscopy (MS) are the two most common spectroscopic analytical techniques employed in metabolomics. The large spectral datasets generated by NMR and MS are often analyzed using data reduction techniques like Principal Component Analysis (PCA). Although rapid, these methods are susceptible to solvent and matrix effects, high rates of false positives, lack of reproducibility and limited data transferability from one platform to the next....
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[NMR paper] Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR
Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR correlation spectra.
Related Articles Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR correlation spectra.
J Biomol NMR. 2003 Mar;25(3):217-23
Authors: van Rossum BJ, Castellani F, Pauli J, Rehbein K, Hollander J, de Groot HJ, Oschkinat H
In this paper, we present a strategy for the (1)H(N) resonance assignment in solid-state magic-angle spinning (MAS) NMR, using the alpha-spectrin SH3 domain as an example. A novel 3D...
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[NMR paper] Tools for the automated assignment of high-resolution three-dimensional protein NMR s
Tools for the automated assignment of high-resolution three-dimensional protein NMR spectra based on pattern recognition techniques.
Tools for the automated assignment of high-resolution three-dimensional protein NMR spectra based on pattern recognition techniques.
J Biomol NMR. 1997 Oct;10(3):207-19
Authors: Croft D, Kemmink J, Neidig KP, Oschkinat H
One of the major bottlenecks in the determination of proteinstructures by NMR is in the evaluation of the data produced by theexperiments. An important step in this process is assignment, where...
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[NMR paper] 13C and proton NMR studies of horse cytochrome c. Systematic assignment of methyl and
13C and proton NMR studies of horse cytochrome c. Systematic assignment of methyl and methine resonances in both oxidation states.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 13C and proton NMR studies of horse cytochrome c. Systematic assignment of methyl and methine resonances in both oxidation states.
Eur J Biochem. 1992 Jun 15;206(3):721-8
Authors: Santos H, Turner DL
The CHn groups in the aliphatic side chains of horse...
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[NMR paper] High resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspa
High resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspartic acids and structural implications of single site mutations.
Related Articles High resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspartic acids and structural implications of single site mutations.
Eur Biophys J. 1990;18(1):17-24
Authors: Engelhard M, Hess B, Metz G, Kreutz W, Siebert F, Soppa J, Oesterhelt D
Three mutant strains of Halobacterium sp. GRB with the site of mutation in the bacterioopsin gene (PM 326:...
Low resolution (1)H NMR assignment of proton populations in pound cake and its polymeric ingredients.
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