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Password Structural basis for the ethanol action on G-protein–activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy - pnas.org Sep 06, 2024 - 12:19 PM - by nmrlearner Structural basis for the ethanol action on G-protein–activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy - pnas.org Structural basis for the ethanol action on G-protein–activated inwardly rectifying potassium channel 1 revealed by NMR spectroscopy pnas.org Read here 0 Replies | 203 Views Equilibrium NMR studies of unfolded and partially folded proteins - Nature.com Sep 04, 2024 - 8:59 AM - by nmrlearner Equilibrium NMR studies of unfolded and partially folded proteins - Nature.com Equilibrium NMR studies of unfolded and partially folded proteins Nature.com Read here 0 Replies | 107 Views The molecular basis for protein kinase A anchoring revealed by solution NMR - Nature.com Sep 03, 2024 - 5:00 AM - by nmrlearner The molecular basis for protein kinase A anchoring revealed by solution NMR - Nature.com The molecular basis for protein kinase A anchoring revealed by solution NMR Nature.com Read here 0 Replies | 104 Views [NMR paper] Lysine methylation: A strategy to improve in-cell NMR spectroscopy of proteins Sep 02, 2024 - 2:55 PM - by nmrlearner Lysine methylation: A strategy to improve in-cell NMR spectroscopy of proteins BACKGROUND: In-cell NMR is a valuable technique for investigating protein structure and function in cellular environments. However, challenges arise due to highly crowded cellular environment, where nonspecific interactions between the target protein and other cellular components can lead to signals broadening or disappearance in NMR spectra. More... 0 Replies | 758 Views [NMR paper] Solution NMR backbone resonance assignment of the full-length resistance-related calcium-binding protein Sorcin Sep 02, 2024 - 2:54 AM - by nmrlearner Solution NMR backbone resonance assignment of the full-length resistance-related calcium-binding protein Sorcin Sorcin is a penta-EF hand calcium-binding protein that confers multidrug resistance in cancer cells. It regulates cellular Ca^(2+) homeostasis by interacting with calcium channels such as Ryanodine receptor 2 and Sarcoplasmic/endoplasmic reticulum Ca^(2+)-ATPase in a calcium-dependent manner. The crystal structure of the Sorcin has been determined in both calcium-free and calcium-bound states to understand calcium-binding induced conformational change. However, due to its flexibility, most of... More... 0 Replies | 117 Views [NMR paper] Solution NMR backbone assignment of the N-terminal tandem Zalpha1-Zalpha2 domains of Z-DNA binding protein 1 Sep 02, 2024 - 2:54 AM - by nmrlearner Solution NMR backbone assignment of the N-terminal tandem Zalpha1-Zalpha2 domains of Z-DNA binding protein 1 The detection of nucleic acids that are present in atypical conformations is a crucial trigger of the innate immune response. Human Z-DNA binding protein 1 (ZBP1) is a pattern recognition receptor that harbors two Z? domains that recognize Z-DNA and Z-RNA. ZBP1 detects this alternate nucleic acid conformation as foreign, and upon stabilization of these substrates, it triggers activation of an immune response. Here, we present the backbone chemical shift assignment of a construct encompassing the... More... 0 Replies | 80 Views Pitfalls in measurements of R1 relaxation rates of protein backbone 15N nuclei Sep 01, 2024 - 2:47 PM - by nmrlearner Pitfalls in measurements of R1 relaxation rates of protein backbone 15N nuclei Abstract The dynamics of the backbone and side-chains of protein are routinely studied by interpreting experimentally determined 15N spin relaxation rates. R1(15N), the longitudinal relaxation rate, reports on fast motions and encodes, together with the transverse relaxation R2, structural information about the shape of the molecule and the orientation of the amide bond vectors in the internal diffusion frame. Determining error-free 15N longitudinal relaxation rates remains a challenge for small, disordered, and medium-sized proteins. Here, we show that mono-exponential fitting is sufficient, with no statistical preference for bi-exponential fitting up to 800Â*MHz. A detailed comparison of the TROSY and HSQC techniques at medium and high fields showed no statistically significant differences. The least error-prone DD/CSA interference removal technique is the selective inversion of amide signals while avoiding water resonance. The exchange of amide with solvent deuterons appears to affect the rate R1 of solvent-exposed amides in all fields tested and in each DD/CSA interference removal technique in a statistically significant manner. In summary, the most accurate R1(15N) rates in proteins are achieved by selective amide inversion, without the addition of D2O. Importantly, at high magnetic fields stronger than 800Â*MHz, when non-mono-exponential decay is involved, it is advisable to consider elimination of the shortest delays (typically up to 0.32Â*s) or bi-exponential fitting. ... [Read More] 0 Replies | 141 Views NMR Structure Determination for Larger Proteins Using Backbone-Only Data - Science Sep 01, 2024 - 1:51 AM - by nmrlearner NMR Structure Determination for Larger Proteins Using Backbone-Only Data - Science NMR Structure Determination for Larger Proteins Using Backbone-Only Data Science Read here 0 Replies | 135 Views Page 51 of 100 « First < 41 49 50 51 52 53 61 > Last »

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