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» Welcome! Welcome, NMR world! Our visitors map. » Log in User Name Remember Me? Not a member yet? Register Now! Password Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal ... - Nature.com Feb 16, 2024 - 7:14 AM - by nmrlearner Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal ... - Nature.com Structural transitions in full-length human prion protein detected by xenon as probe and spin labeling of the N-terminal ... Nature.com Read here 0 Replies | 67 Views [NMR paper] The NMR structure of the Orf63 lytic developmental protein from lambda bacteriophage Feb 16, 2024 - 7:14 AM - by nmrlearner The NMR structure of the Orf63 lytic developmental protein from lambda bacteriophage The orf63 gene resides in a region of the lambda bacteriophage genome between the exo and xis genes and is among the earliest genes transcribed during infection. In lambda phage and Shiga toxin (Stx) producing phages found in enterohemorrhagic Escherichia coli (EHEC) associated with food poisoning, Orf63 expression reduces the host survival and hastens the period between infection and lysis thereby giving it pro-lytic qualities. The NMR structure of dimeric Orf63 reveals a fold consisting of two... More... 0 Replies | 207 Views [NMR paper] The role of NMR in advancing small molecule drug discovery Feb 16, 2024 - 7:14 AM - by nmrlearner The role of NMR in advancing small molecule drug discovery Navigating the ever-evolving landscape of nuclear magnetic resonance (NMR) poses challenges for the industry. This work explores promising approaches that illuminate protein-ligand interactions in the context of structural dynamics, facilitating targeted drug discovery. I acknowledge existing limitations and highlight future opportunities, which may pave the way for broader NMR integration and faster therapeutic development. More... 0 Replies | 72 Views [NMR paper] Probing the dynamic landscape of peptides in molecular assemblies by synergized NMR experiments and MD simulations Feb 16, 2024 - 7:14 AM - by nmrlearner Probing the dynamic landscape of peptides in molecular assemblies by synergized NMR experiments and MD simulations Peptides or proteins containing small biomolecular aggregates, such as micelles, bicelles, droplets and nanodiscs, are pivotal in many fields ranging from structural biology to pharmaceutics. Monitoring dynamics of such systems has been limited by the lack of experimental methods that could directly detect their fast (picosecond to nanosecond) timescale dynamics. Spin relaxation times from NMR experiments are sensitive to such motions, but their interpretation for biomolecular aggregates is not... More... 0 Replies | 63 Views [NMR paper] Solution NMR Analysis of O-Glycopeptide-Antibody Interaction Feb 16, 2024 - 7:14 AM - by nmrlearner Solution NMR Analysis of O-Glycopeptide-Antibody Interaction O-Linked glycans potentially play a functional role in cellular recognition events. Recent structural analyses suggest that O-glycosylation can be a specific signal for a lectin receptor which recognizes both the O-glycan and the adjacent polypeptide region. Further, certain antibodies specifically bind to the O-glycosylated peptide. There is growing interest in the mechanism by which O-glycans on proteins are specifically recognized by lectins and antibodies. The recognition system may be... More... 0 Replies | 68 Views [NMR paper] NMR and Single-Molecule FRET Insights into Fast Protein Motions and Their Relation to Function Feb 16, 2024 - 7:14 AM - by nmrlearner NMR and Single-Molecule FRET Insights into Fast Protein Motions and Their Relation to Function Proteins often undergo large-scale conformational transitions, in which secondary and tertiary structure elements (loops, helices, and domains) change their structures or their positions with respect to each other. Simple considerations suggest that such dynamics should be relatively fast, but the functional cycles of many proteins are often relatively slow. Sophisticated experimental methods are starting to tackle this dichotomy and shed light on the contribution of large-scale conformational... More... 0 Replies | 61 Views [NMR paper] Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures Feb 16, 2024 - 7:14 AM - by nmrlearner Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures While low-temperature Nuclear Magnetic Resonance (NMR) holds great promise for the analysis of unstable samples and for sensitizing NMR detection, spectral broadening in frozen protein samples is a common experimental challenge. One hypothesis explaining the additional linewidth is that a variety of conformations are in rapid equilibrium at room temperature and become frozen, creating an inhomogeneous distribution at cryogenic temperatures. Here, we investigate conformational heterogeneity by... More... 0 Replies | 69 Views [NMR paper] Using Abundant 1H Polarization to Enhance the Sensitivity of Solid-State NMR Spectroscopy Feb 16, 2024 - 7:14 AM - by nmrlearner Using Abundant 1H Polarization to Enhance the Sensitivity of Solid-State NMR Spectroscopy Solid-state NMR spectroscopy has been playing a significant role in elucidating the structures and dynamics of materials and proteins at the atomic level for decades. As an extremely abundant nucleus with a very high gyromagnetic ratio, protons are widely present in most organic/inorganic materials. Thus, this Perspective highlights the advantages of proton detection at fast magic-angle spinning (MAS) and presents strategies to utilize and exhaust ¹H polarization to achieve signal sensitivity... More... 0 Replies | 219 Views Page 23 of 100 « First < 13 21 22 23 24 25 33 73 > Last »

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