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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] Enhanced TROSY Effect In [2-19F, 2-13C] Adenosine and ATP Analogs Facilitates NMR Spectroscopy of Very Large Biological RNAs in Solution Jan 08, 2024 - 3:07 PM - by nmrlearner Enhanced TROSY Effect In [2-19F, 2-13C] Adenosine and ATP Analogs Facilitates NMR Spectroscopy of Very Large Biological RNAs in Solution Large RNAs are central to cellular functions, and yet characterizing such RNAs remains outside the reach of solution NMR. We present two labeling technologies based on [2-19F, 2-13C]-adenosine, which allow the incorporation of aromatic 19F-13C spin pairs. The labels when coupled with the powerful transverse relaxation optimized spectroscopy (TROSY) enable us to probe RNAs comprising up to 124 nucleotides. With our new [2-19F, 2-13C]-adenosine-phosphoramidite, all resonances of the human... More... 0 Replies | 259 Views [NMR paper] The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis Jan 06, 2024 - 5:03 PM - by nmrlearner The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis Multidimensional NMR spectra are the basis for studying proteins by NMR spectroscopy and crucial for the development and evaluation of methods for biomolecular NMR data analysis. Nevertheless, in contrast to derived data such as chemical shift assignments in the BMRB and protein structures in the PDB databases, this primary data is in general not publicly archived. To change this unsatisfactory situation, we present a standardized set of solution NMR data comprising 1329 2-4-dimensional NMR... More... 0 Replies | 318 Views Beyond slow two-state protein conformational exchange using CEST: applications to three-state protein interconversion on the millisecond timescale Jan 03, 2024 - 3:00 PM - by nmrlearner Beyond slow two-state protein conformational exchange using CEST: applications to three-state protein interconversion on the millisecond timescale Abstract Although NMR spectroscopy is routinely used to study the conformational dynamics of biomolecules, robust analyses of the data are challenged in cases where exchange is more complex than two-state, such as when a â??visibleâ?? major conformer exchanges with two â??invisibleâ?? minor states on the millisecond timescale. It is becoming increasingly clear that chemical exchange saturation transfer (CEST) NMR experiments that were initially developed to study systems undergoing slow interconversion are also sensitive to intermediateâ??fast timescale biomolecular conformational exchange. Here we investigate the utility of the amide 15N CEST experiment to characterise protein three-state exchange occurring on the millisecond timescale by studying the interconversion between the folded (F) state of the FF domain from human HYPA/FBP11 (WT FF) and two of its folding intermediates I1 and I2. Although 15N CPMG experiments are consistent with the F state interconverting with a single minor state on the millisecond timescale, 15N CEST data clearly establish an exchange process between F and a pair of minor states. A unique three-state exchange model cannot be obtained by analysis of 15N CEST data recorded at a single temperature. However, including the relative sign of the difference in the chemical shifts of the two minor states based on a simple two-state analysis of CEST data recorded at multiple temperatures, results in a robust three-state model in which the F, I1 and I2 states interconvert with each other on the millisecond timescale ( ... [Read More] 0 Replies | 470 Views [NMR paper] Speeding-up the Determination of Protein-Ligand Affinities by STD NMR: The Reduced Data Set STD NMR Approach (rd-STD NMR) Jan 03, 2024 - 1:39 AM - by nmrlearner Speeding-up the Determination of Protein-Ligand Affinities by STD NMR: The Reduced Data Set STD NMR Approach (rd-STD NMR) STD NMR spectroscopy is a powerful ligand-observed NMR tool for screening and characterizing the interactions of small molecules and low molecular weight fragments with a given macromolecule, identifying the main intermolecular contacts in the bound state. It is also a powerful analytical technique for the accurate determination of protein-ligand dissociation constants (K(D)) of medium-to-weak affinity, of interest in the pharmaceutical industry. However, accurate K(D) determination and epitope... More... 0 Replies | 229 Views Using Fluorescence Microscopy to Study Proteins - News-Medical.Net Dec 29, 2023 - 3:15 PM - by nmrlearner Using Fluorescence Microscopy to Study Proteins - News-Medical.Net Using Fluorescence Microscopy to Study Proteins News-Medical.Net Read here 0 Replies | 298 Views [NMR paper] Membrane Protein Structures in Native Cellular Membranes Revealed by Solid-State NMR Spectroscopy Dec 29, 2023 - 3:15 PM - by nmrlearner Membrane Protein Structures in Native Cellular Membranes Revealed by Solid-State NMR Spectroscopy The structural characterization of membrane proteins within the cellular membrane environment is critical for understanding the molecular mechanism in their native functional context. However, conducting residue site-specific structural analysis of membrane proteins in native membranes by solid-state NMR faces challenges due to poor spectral sensitivity and serious interference from background protein signals. In this study, we present a new protocol that combines various strategies for cellular... More... 0 Replies | 492 Views 19F NMR viewed through two different lenses: ligand-observed and protein-observed 19F NMR applications for ... - ScienceDirect Dec 28, 2023 - 10:50 PM - by nmrlearner 19F NMR viewed through two different lenses: ligand-observed and protein-observed 19F NMR applications for ... - ScienceDirect 19F NMR viewed through two different lenses: ligand-observed and protein-observed 19F NMR applications for ... ScienceDirect Read here 0 Replies | 185 Views Assignment and secondary structure of the YadA membrane protein by solid-state MAS NMR | Scientific Reports - Nature.com Dec 28, 2023 - 10:50 PM - by nmrlearner Assignment and secondary structure of the YadA membrane protein by solid-state MAS NMR | Scientific Reports - Nature.com Assignment and secondary structure of the YadA membrane protein by solid-state MAS NMR | Scientific Reports Nature.com Read here 0 Replies | 201 Views Page 34 of 100 « First < 24 32 33 34 35 36 44 84 > Last »

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