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» Welcome! Welcome, NMR world! Our visitors map. » Log in User Name Remember Me? Not a member yet? Register Now! Password Solid-state NMR structure determination of a membrane protein in E ... - Science Nov 02, 2023 - 12:38 PM - by nmrlearner Solid-state NMR structure determination of a membrane protein in E ... - Science Solid-state NMR structure determination of a membrane protein in E ... Science Read here 0 Replies | 170 Views Revealing structural secrets of key cancer protein - Mirage News Nov 02, 2023 - 12:38 PM - by nmrlearner Revealing structural secrets of key cancer protein Mirage News Revealing structural secrets of key cancer protein - Mirage News More... 0 Replies | 220 Views Dimeric Transmembrane Structure of the SARS-CoV-2 E Protein ... - Nature.com Nov 01, 2023 - 3:27 PM - by nmrlearner Dimeric Transmembrane Structure of the SARS-CoV-2 E Protein ... - Nature.com Dimeric Transmembrane Structure of the SARS-CoV-2 E Protein ... Nature.com Read here 0 Replies | 211 Views [NMR paper] B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles Nov 01, 2023 - 3:27 PM - by nmrlearner B2LiVe, a label-free 1D-NMR method to quantify the binding of amphitropic peptides or proteins to membrane vesicles Amphitropic proteins and peptides reversibly partition from solution to membrane, a key process that regulates their functions. Experimental approaches classically used to measure protein partitioning into lipid bilayers, such as fluorescence and circular dichroism, are hardly usable when the peptides or proteins do not exhibit significant polarity and/or conformational changes upon membrane binding. Here, we describe binding to lipid vesicles (B2LiVe), a simple, robust, and widely applicable... More... 0 Replies | 204 Views [NMR paper] A 19F-qNMR-Guided Mathematical Model for G Protein-Coupled Receptor Signaling Nov 01, 2023 - 3:27 PM - by nmrlearner A 19F-qNMR-Guided Mathematical Model for G Protein-Coupled Receptor Signaling GPCRs exhibit a wide range of pharmacological efficacies, yet the molecular mechanisms responsible for the differential efficacies in response to various ligands remain poorly understood. This lack of understanding has hindered the development of a solid foundation for establishing a mathematical model for signaling efficacy. However, recent progress has been made in delineating and quantifying receptor conformational states and associating function with these conformations. This progress has... More... 0 Replies | 154 Views [NMR paper] Exploring Sulfur Sites in Proteins via Triple-Resonance 1H-Detected 77Se NMR Nov 01, 2023 - 2:23 AM - by nmrlearner Exploring Sulfur Sites in Proteins via Triple-Resonance 1H-Detected 77Se NMR NMR spectroscopy has been applied to virtually all sites within proteins and biomolecules; however, the observation of sulfur sites remains very challenging. Recent studies have examined ^(77)Se as a replacement for sulfur and applied ^(77)Se NMR in both the solution and solid states. As a spin-1/2 nuclide, ^(77)Se is attractive as a probe of sulfur sites, and it has a very large chemical shift range (due to a large chemical shift anisotropy), which makes it potentially very sensitive to... More... 0 Replies | 160 Views [NMR paper] Towards resolving the complex paramagnetic nuclear magnetic resonance (NMR) spectrum of small laccase: assignments of resonances to residue-specific nuclei Oct 31, 2023 - 10:49 AM - by nmrlearner Towards resolving the complex paramagnetic nuclear magnetic resonance (NMR) spectrum of small laccase: assignments of resonances to residue-specific nuclei Laccases efficiently reduce dioxygen to water in an active site containing a tri-nuclear copper centre (TNC). The dynamics of the protein matrix is a determining factor in the efficiency in catalysis. To probe mobility, nuclear magnetic resonance (NMR) spectroscopy is highly suitable. However, several factors complicate the assignment of resonances to active site nuclei in laccases. The paramagnetic nature causes large shifts and line broadening. Furthermore, the presence of slow chemical... More... 0 Replies | 120 Views [NMR paper] The long-standing relationship between paramagnetic NMR and iron-sulfur proteins: the mitoNEET example. An old method for new stories or the other way around? Oct 31, 2023 - 10:49 AM - by nmrlearner The long-standing relationship between paramagnetic NMR and iron-sulfur proteins: the mitoNEET example. An old method for new stories or the other way around? Paramagnetic NMR spectroscopy and iron-sulfur (Fe-S) proteins have maintained a synergic relationship for decades. Indeed, the hyperfine shifts with their temperature dependencies and the relaxation rates of nuclei of cluster-bound residues have been extensively used as a fingerprint of the type and of the oxidation state of the Fe-S cluster within the protein frame. The identification of NMR signals from residues surrounding the metal cofactor is crucial for understanding the structure-function... More... 0 Replies | 136 Views Page 47 of 100 « First < 37 45 46 47 48 49 57 97 > Last »

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