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» Welcome! Welcome, NMR world! Our visitors map. » Log in User Name Remember Me? Not a member yet? Register Now! Password DNP-assisted solid-state NMR enables detection of proteins at nanomolar concentrations in fully protonated cellular milieu Mar 24, 2024 - 6:32 AM - by nmrlearner DNP-assisted solid-state NMR enables detection of proteins at nanomolar concentrations in fully protonated cellular milieu Abstract With the sensitivity enhancements conferred by dynamic nuclear polarization (DNP), magic angle spinning (MAS) solid state NMR spectroscopy experiments can attain the necessary sensitivity to detect very low concentrations of proteins. This potentially enables structural investigations of proteins at their endogenous levels in their biological contexts where their native stoichiometries with potential interactors is maintained. Yet, even with DNP, experiments are still sensitivity limited. Moreover, when an isotopically-enriched target protein is present at physiological levels, which typically range from low micromolar to nanomolar concentrations, the isotope content from the natural abundance isotopes in the cellular milieu can outnumber the isotope content of the target protein. Using isotopically enriched yeast prion protein, Sup35NM, diluted into natural abundance yeast lysates, we optimized sample composition. We found that modest cryoprotectant concentrations and fully protonated environments support efficient DNP. We experimentally validated theoretical calculations of the limit of specificity for an isotopically enriched protein in natural abundance cellular milieu. We establish that, using pulse sequences that are selective for adjacent NMR-active nuclei, proteins can be specifically detected in cellular milieu at concentrations in the hundreds of nanomolar. Finally, we find that maintaining native stoichiometries of the protein of interest to the components of the cellular environment may be important for proteins that make specific interactions with cellular... [Read More] 0 Replies | 146 Views Decorating phenylalanine side-chains with triple labeled 13C/19F/2H isotope patterns Mar 24, 2024 - 6:32 AM - by nmrlearner Decorating phenylalanine side-chains with triple labeled 13C/19F/2H isotope patterns Abstract We present an economic and straightforward method to introduce 13C-19F spin systems into the deuterated aromatic side chains of phenylalanine as reporters for various protein NMR applications. The method is based on the synthesis of [4-13C, 2,3,5,6-2H4] 4-fluorophenylalanine from the commercially available isotope sources [2-13C] acetone and deuterium oxide. This compound is readily metabolized by standard Escherichia coli overexpression in a glyphosate-containing minimal medium, which results in high incorporation rates in the corresponding target proteins. Source: Journal of Biomolecular NMR 0 Replies | 49 Views Quantifying acute-phase inflammation proteins by nuclear magnetic resonance spectrometry - Medical Xpress Mar 24, 2024 - 6:32 AM - by nmrlearner Quantifying acute-phase inflammation proteins by nuclear magnetic resonance spectrometry Medical Xpress Quantifying acute-phase inflammation proteins by nuclear magnetic resonance spectrometry - Medical Xpress More... 0 Replies | 67 Views Nuclear magnetic resonance scanner for individual proteins - mpg.de Mar 24, 2024 - 6:32 AM - by nmrlearner Nuclear magnetic resonance scanner for individual proteins mpg.de Nuclear magnetic resonance scanner for individual proteins - mpg.de More... 0 Replies | 55 Views Molecular basis of ?-lactam antibiotic resistance of ESKAPE bacterium E. faecium Penicillin Binding Protein PBP5 - Nature.com Mar 24, 2024 - 6:32 AM - by nmrlearner Molecular basis of ?-lactam antibiotic resistance of ESKAPE bacterium E. faecium Penicillin Binding Protein PBP5 - Nature.com Molecular basis of ?-lactam antibiotic resistance of ESKAPE bacterium E. faecium Penicillin Binding Protein PBP5 Nature.com Read here 0 Replies | 67 Views NMR methods for exploring 'dark' states in ligand binding and protein-protein interactions - ScienceDirect.com Mar 24, 2024 - 6:32 AM - by nmrlearner NMR methods for exploring 'dark' states in ligand binding and protein-protein interactions - ScienceDirect.com NMR methods for exploring 'dark' states in ligand binding and protein-protein interactions ScienceDirect.com Read here 0 Replies | 67 Views The NMR structure of the engineered halophilic DnaE intein for segmental isotopic labeling using conditional protein ... - ScienceDirect.com Mar 24, 2024 - 6:32 AM - by nmrlearner The NMR structure of the engineered halophilic DnaE intein for segmental isotopic labeling using conditional protein ... - ScienceDirect.com The NMR structure of the engineered halophilic DnaE intein for segmental isotopic labeling using conditional protein ... ScienceDirect.com Read here 0 Replies | 74 Views Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2 - Nature.com Mar 24, 2024 - 6:32 AM - by nmrlearner Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2 - Nature.com Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2 Nature.com Read here 0 Replies | 67 Views Page 10 of 100 « First < 8 9 10 11 12 20 60 > Last »

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