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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 paper] Investigating Different Dynamic pHP1alpha States in Their KCl-Mediated Liquid-Liquid Phase Separation (LLPS) Using Solid-State NMR (SSNMR) and Molecular Dynamic (MD) Simulations Oct 15, 2024 - 11:40 PM - by nmrlearner Investigating Different Dynamic pHP1alpha States in Their KCl-Mediated Liquid-Liquid Phase Separation (LLPS) Using Solid-State NMR (SSNMR) and Molecular Dynamic (MD) Simulations Chromatin phase separation is dynamically regulated by many factors, such as post-translational modifications and effector proteins, and plays a critical role in genomic activities. The liquid-liquid phase separation (LLPS) of chromatin and/or effector proteins has been observed both in vitro and in vivo. However, the underlying mechanisms are largely unknown, and elucidating the physicochemical properties of the phase-separated complexes remains technically challenging. In this study, we... More... 0 Replies | 69 Views [NMR paper] High-Sensitivity Analysis of Native Bacterial Biofilms Using Dynamic Nuclear Polarization-Enhanced Solid-State NMR Oct 15, 2024 - 11:40 PM - by nmrlearner High-Sensitivity Analysis of Native Bacterial Biofilms Using Dynamic Nuclear Polarization-Enhanced Solid-State NMR Bacterial biofilms cause persistent infections that are difficult to treat and contribute greatly to antimicrobial resistance. However, high-resolution structural information on native bacterial biofilms remain very limited. This limitation is primarily due to methodological constraints associated with analyzing complex native samples. Although solid-state NMR (ssNMR) is a promising method in this regard, its conventional applications typically suffer from sensitivity limitations, particularly... More... 0 Replies | 54 Views [NMR paper] Optimization of (15)N-(13)C double-resonance NMR experiments under low temperature magic angle spinning dynamic nuclear polarization conditions Oct 15, 2024 - 11:40 PM - by nmrlearner Optimization of (15)N-(13)C double-resonance NMR experiments under low temperature magic angle spinning dynamic nuclear polarization conditions Dynamic nuclear polarization (DNP) enhanced magic angle spinning (MAS) solid-state NMR carried out at 25 K enables rapid acquisition of multi-dimensional ^(13)C-^(15)N correlation spectra for protein structure studies and resonance assignment. Under commonly used DNP conditions, solvent deuteration reduces ¹H-^(15)N cross polarization (CP) efficiencies, necessitates more careful optimization, and requires longer high-power ^(15)N radio-frequency pulses. The sensitivity of 2D heteronuclear... More... 0 Replies | 57 Views [NMR paper] Ultrafast T(1)-T(1rho) NMR for Correlating Different Motional Regimes of Molecules Oct 15, 2024 - 11:40 PM - by nmrlearner Ultrafast T(1)-T(1rho) NMR for Correlating Different Motional Regimes of Molecules Nuclear magnetic resonance (NMR) relaxation times provide detailed information about molecular motions and local chemical environments. Longitudinal T(1) relaxation time is most often sensitive to relatively fast, nano- to picosecond ranges of molecular motion. Rotating frame T(1?) relaxation time reflects a much slower, micro- to millisecond range of motion, and the motional regime can be tuned by changing spin-lock field strength. Conventional methods for measuring T(1) and T(1?) relaxation... More... 0 Replies | 50 Views [NMR paper] Evaluating protocols for reproducible targeted metabolomics by NMR Oct 15, 2024 - 11:40 PM - by nmrlearner Evaluating protocols for reproducible targeted metabolomics by NMR Metabolomics aims to study the downstream effects of variables like diet, environment, or disease on a given biological system. However, inconsistencies in sample preparation, data acquisition/processing protocols lead to reproducibility and accuracy concerns. A systematic study was conducted to assess how sample preparation methods and data analysis platforms affect metabolite susceptibility. A targeted panel of 25 metabolites was evaluated in 69 clinical metabolomics samples prepared following... More... 0 Replies | 55 Views [NMR paper] Disentangling the Complexity in Protein Complexes Using Complementary Isotope-Labeling and Multiple-Receiver NMR Spectroscopy Oct 15, 2024 - 11:40 PM - by nmrlearner Disentangling the Complexity in Protein Complexes Using Complementary Isotope-Labeling and Multiple-Receiver NMR Spectroscopy Intrinsically disordered proteins are abundant in eukaryotic systems, but they remain largely elusive pharmacological targets. NMR spectroscopy proved to be a suitable method to study these proteins and their interaction with one another or with drug candidates. Although NMR can give atomistic information about these interplays, molecular complexity due to severe spectral overlap, limited sample stability, and quantity remain an issue and hamper widespread applications. Here, we propose an... More... 0 Replies | 83 Views [NMR paper] Exploring the dynamics and interactions of the N-myc transactivation domain through solution NMR Oct 15, 2024 - 11:40 PM - by nmrlearner Exploring the dynamics and interactions of the N-myc transactivation domain through solution NMR Myc proteins are transcription factors crucial for cell proliferation. They have a C-terminal domain that mediates Max and DNA binding, and an N-terminal disordered region culminating in the transactivation domain (TAD). The TAD participates in many protein-protein interactions, notably with kinases that promote stability (Aurora-A) or degradation (ERK1, GSK3) via the ubiquitin-proteasome system. We probed the structure, dynamics and interactions of N-myc TAD using nuclear magnetic resonance... More... 0 Replies | 50 Views [NMR paper] Structural changes of Natronomonas pharaonis halorhodopsin in its late photocycle revealed by solid-state NMR spectroscopy Oct 15, 2024 - 11:40 PM - by nmrlearner Structural changes of Natronomonas pharaonis halorhodopsin in its late photocycle revealed by solid-state NMR spectroscopy Natronomonas pharaonis halorhodopsin (NpHR) is a light-driven Cl^(-) inward pump that is widely used as an optogenetic tool. Although NpHR is previously extensively studied, its Cl^(-) uptake process is not well understood from the protein structure perspective, mainly because in crystalline lattice, it has been difficult to analyze the structural changes associated with the Cl^(-) uptake process. In this study, we used solid-state NMR to analyze NpHR both in the Cl^(-)-bound and -free states... More... 0 Replies | 88 Views Page 41 of 100 « First < 31 39 40 41 42 43 51 91 > Last »

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