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» Welcome! Welcome, NMR world! Our visitors map. » Log in User Name Remember Me? Not a member yet? Register Now! Password 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 | 64 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 | 70 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 | 63 Views Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR - Nature.com Mar 24, 2024 - 6:32 AM - by nmrlearner Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR - Nature.com Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR Nature.com Read here 0 Replies | 70 Views Efficient and economic protein labeling for NMR in mammalian expression systems: Application to a preT-cell and T-cell receptor protein Mar 24, 2024 - 6:32 AM - by nmrlearner Efficient and economic protein labeling for NMR in mammalian expression systems: Application to a preT-cell and T-cell receptor protein Abstract Protein nuclear magnetic resonance*(NMR) spectroscopy relies on the ability to isotopically label polypeptides, which is achieved through heterologous expression in various host organisms. Most commonly, Escherichia coli is employed by leveraging isotopically substituted ammonium and glucose to uniformly label proteins with 15N and 13C, respectively. Moreover, E. coli can grow and express proteins in uniformly deuterium-substituted water (D2O), a strategy useful for experiments targeting high molecular weight proteins. Unfortunately, many proteins, particularly those requiring specific posttranslational modifications like disulfide bonding or glycosylation for proper folding and/or function, cannot be readily expressed in their functional forms using E. coli-based expression systems. One such class of proteins includes T-cell receptors and their related preT-cell receptors. In this study, we present an expression system for isotopic labeling of proteins using a nonadherent human embryonic kidney cell line, Expi293F, and a specially designed media. We demonstrate the application of this platform to the ? subunit common to both receptors. In addition, we show that this expression system and media can be used to specifically label amino acids Phe, Ile, Val, and Leu in this system, utilizing an amino acid-specific labeling protocol that allows targeted incorporation at high efficiency without significant isotopic scrambling. We demonstrate that this system can also be used to express proteins with fluorinated amino acids. We were routinely able to obtain an NMR... [Read More] 0 Replies | 58 Views Xplor-NIH: Better parameters and protocols for NMR protein structure determination Mar 24, 2024 - 6:32 AM - by nmrlearner Xplor-NIH: Better parameters and protocols for NMR protein structure determination Abstract The present work describes an update to the protein covalent geometry and atomic radii parameters in the Xplor-NIH biomolecular structure determination package. In combination with an improved treatment of selected non-bonded interactions between atoms three bonds apart, such as those involving methyl hydrogens, and a previously developed term that affects the system's gyration volume, the new parameters are tested using structure calculations on 30 proteins with restraints derived from nuclear magnetic resonance data. Using modern structure validation criteria, including several formally adopted by the Protein Data Bank, and a clear measure of structural accuracy, the results show superior performance relative to previous Xplor-NIH implementations. Additionally, the Xplor-NIH structures compare favorably against originally determined NMR models. More... 0 Replies | 67 Views [NMR paper] 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 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.... More... 0 Replies | 66 Views [NMR paper] Efficient and economic protein labeling for NMR in mammalian expression systems: Application to a preT-cell and T-cell receptor protein Mar 24, 2024 - 6:32 AM - by nmrlearner Efficient and economic protein labeling for NMR in mammalian expression systems: Application to a preT-cell and T-cell receptor protein Protein nuclear magnetic resonance (NMR) spectroscopy relies on the ability to isotopically label polypeptides, which is achieved through heterologous expression in various host organisms. Most commonly, Escherichia coli is employed by leveraging isotopically substituted ammonium and glucose to uniformly label proteins with ^(15)N and ^(13)C, respectively. Moreover, E. coli can grow and express proteins in uniformly deuterium-substituted water (D(2)O), a strategy useful for experiments targeting... More... 0 Replies | 66 Views Page 8 of 100 « First < 6 7 8 9 10 18 58 > Last »

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