[NMR paper] Absolute nutrient concentration measurements in cell culture media: (1)H q-NMR spectra and data to compare the efficiency of pH-controlled protein precipitation versus CPMG or post-processing filtering approaches.
Absolute nutrient concentration measurements in cell culture media: (1)H q-NMR spectra and data to compare the efficiency of pH-controlled protein precipitation versus CPMG or post-processing filtering approaches.
Absolute nutrient concentration measurements in cell culture media: (1)H q-NMR spectra and data to compare the efficiency of pH-controlled protein precipitation versus CPMG or post-processing filtering approaches.
Data Brief. 2016 Sep;8:387-93
Authors: Goldoni L, Beringhelli T, Rocchia W, Realini N, Piomelli D
Abstract
The NMR spectra and data reported in this article refer to the research article titled "A simple and accurate protocol for absolute polar metabolite quantification in cell cultures using q-NMR" [1]. We provide the (1)H q-NMR spectra of cell culture media (DMEM) after removal of serum proteins, which show the different efficiency of various precipitating solvents, the solvent/DMEM ratios, and pH of the solution. We compare the data of the absolute nutrient concentrations, measured by PULCON external standard method, before and after precipitation of serum proteins and those obtained using CPMG (Carr-Purcell-Meiboom-Gill) sequence or applying post-processing filtering algorithms to remove, from the (1)H q-NMR spectra, the proteins signal contribution. For each of these approaches, the percent error in the absolute value of every measurement for all the nutrients is also plotted as accuracy assessment.
[NMR paper] Profiling sulfation/epimerization pattern of full-length heparan sulfate by NMR following cell culture 13C-glucose metabolic labeling.
Profiling sulfation/epimerization pattern of full-length heparan sulfate by NMR following cell culture 13C-glucose metabolic labeling.
Related Articles Profiling sulfation/epimerization pattern of full-length heparan sulfate by NMR following cell culture 13C-glucose metabolic labeling.
Glycobiology. 2014 Oct 21;
Authors: Pegeot M, Sadir R, Eriksson I, Kjellen L, Simorre JP, Gans P, Lortat-Jacob H
Abstract
Through its ability to interact with proteins, heparan sulfate (HS) fulfills a large variety of functions. Protein binding...
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[NMR paper] NMR methods for metabolomics of Mammalian cell culture bioreactors.
NMR methods for metabolomics of Mammalian cell culture bioreactors.
Related Articles NMR methods for metabolomics of Mammalian cell culture bioreactors.
Methods Mol Biol. 2014;1104:223-36
Authors: Aranibar N, Reily MD
Abstract
Metabolomics has become an important tool for measuring pools of small molecules in mammalian cell cultures expressing therapeutic proteins. NMR spectroscopy has played an important role, largely because it requires minimal sample preparation, does not require chromatographic separation, and is quantitative. The...
[NMR paper] Two-dimensional, rotational-echo double-resonance NMR of cell culture metabolism.
Two-dimensional, rotational-echo double-resonance NMR of cell culture metabolism.
Related Articles Two-dimensional, rotational-echo double-resonance NMR of cell culture metabolism.
J Biol Chem. 1993 Oct 5;268(28):20768-71
Authors: McDowell LM, Cohen ER, Schaefer J
Two-dimensional, rotational-echo double-resonance 13C NMR, a new solid-state NMR technique, has been used to show that the relative fluxes of the labeled chemical bond of L-serine along four metabolic pathways (direct purine synthesis, direct glycine incorporation into protein,...
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[NMR paper] Improved efficiency of protein structure calculations from NMR data using the program
Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.
Related Articles Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.
J Biomol NMR. 1991 Nov;1(4):447-56
Authors: Güntert P, Wüthrich K
A new strategy for NMR structure calculations of proteins with the variable target function method (Braun, W. and Go, N. (1985) J. Mol. Biol., 186, 611) is described, which makes use of...
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08-21-2010 11:12 PM
[NMR paper] Improved efficiency of protein structure calculations from NMR data using the program
Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.
Related Articles Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.
J Biomol NMR. 1991 Nov;1(4):447-56
Authors: Güntert P, Wüthrich K
A new strategy for NMR structure calculations of proteins with the variable target function method (Braun, W. and Go, N. (1985) J. Mol. Biol., 186, 611) is described, which makes use of...
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Double quantum filtering homonuclear MAS NMR correlation spectra: a tool for membrane protein studies
Double quantum filtering homonuclear MAS NMR correlation spectra: a tool for membrane protein studies
Jakob J. Lopez, Christoph Kaiser, Sarika Shastri and Clemens Glaubitz
Journal of Biomolecular NMR; 2008; 41(2) pp 97 - 104
Abstract:
13C homonuclear correlation spectra based on proton driven spin diffusion (PDSD) are becoming increasingly important for obtaining distance constraints from multiply labeled biomolecules by MAS NMR. One particular challenging situation arises when such constraints are to be obtained from spectra with a large natural abundance signal background which...