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Biochemistry Seminar: Melanie Cocco, “Protein Dynamics ... - City University of New York
Oct 18, 2023 - 6:17 AM - by nmrlearner
nmrlearner's Avatar Biochemistry Seminar: Melanie Cocco, “Protein Dynamics ... - City University of New York

Biochemistry Seminar: Melanie Cocco, “Protein Dynamics ... City University of New York Read here
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Resolution in Cryogenic Solid State NMR: Challenges and Solutions
Oct 18, 2023 - 6:17 AM - by nmrlearner
nmrlearner's Avatar Resolution in Cryogenic Solid State NMR: Challenges and Solutions

Abstract

NMR at cryogenic temperatures has the potential to provide rich site-specific details regarding biopolymer structure, function, and mechanistic intermediates. Broad spectral lines compared with room temperature NMR can sometimes present practical challenges. A number of hypotheses regarding the origins of line broadening are explored. One frequently considered explanation is the presence of inhomogeneous conformational distributions. Possibly these arise when the facile characteristic motions that occur near room temperature become dramatically slower or "frozen out" at temperatures below the solvent phase change. Recent studies of low temperature spectra harness the distributions in properties in these low temperature spectra to uncover information regarding the conformational ensembles that drive biological function.

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[NMR paper] Biomolecular NMR spectroscopy in the era of artificial intelligence
Oct 18, 2023 - 6:17 AM - by nmrlearner
nmrlearner's Avatar Biomolecular NMR spectroscopy in the era of artificial intelligence

Biomolecular nuclear magnetic resonance (NMR) spectroscopy and artificial intelligence (AI) have a burgeoning synergy. Deep learning-based structural predictors have forever changed structural biology, yet these tools currently face limitations in accurately characterizing protein dynamics, allostery, and conformational heterogeneity. We begin by highlighting the unique abilities of biomolecular NMR spectroscopy to complement AI-based structural predictions toward addressing these knowledge...

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0 Replies | 160 Views
[NMR paper] NMR screening method based on 19F spin-spin relaxation time for analyses of fluorinated compound bound to proteins
Oct 17, 2023 - 3:24 AM - by nmrlearner
nmrlearner's Avatar NMR screening method based on 19F spin-spin relaxation time for analyses of fluorinated compound bound to proteins

NMR screening methods based on ^(19)F spin-spin relaxation time (^(19)F-T(2)) were applied to fluorinated compounds bound to human serum albumin. Diflunisal and fleroxacin (the fluorinated compounds) contain two and three fluorine atoms per molecule, respectively, and are suitable as the model system for ^(19)F NMR analysis. It was shown that ^(19)F-T(2) was more sensitive in monitoring the binding affinity to the target protein than ^(19)F spin-lattice relaxation time (^(19)F-T(1)). The...

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0 Replies | 244 Views
[NMR paper] NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes
Oct 15, 2023 - 2:43 AM - by nmrlearner
nmrlearner's Avatar NMR-Based Characterization of the Interaction between Yeast Oxa1-CTD and Ribosomes

In mitochondria, the major subunits of oxidative phosphorylation complexes are translated by the mitochondrial ribosome (mito-ribosome). The correct insertion and assembly of these subunits into the inner mitochondrial membrane (IMM) are facilitated by mitochondrial oxidase assembly protein 1 (Oxa1) during the translation process. This co-translational insertion process involves an association between the mito-ribosome and the C-terminus of Oxa1 (Oxa1-CTD) Nuclear magnetic resonance (NMR)...

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0 Replies | 311 Views
A Holy Grail — The Prediction of Protein Structure | NEJM - nejm.org
Oct 13, 2023 - 3:16 PM - by nmrlearner
nmrlearner's Avatar A Holy Grail — The Prediction of Protein Structure | NEJM nejm.org
A Holy Grail — The Prediction of Protein Structure | NEJM - nejm.org
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0 Replies | 205 Views
[NMR paper] High and fast: NMR protein-proton side-chain assignments at 160 kHz and 1.2 GHz
Oct 13, 2023 - 3:16 PM - by nmrlearner
nmrlearner's Avatar High and fast: NMR protein-proton side-chain assignments at 160 kHz and 1.2 GHz

The NMR spectra of side-chain protons in proteins provide important information, not only about their structure and dynamics, but also about the mechanisms that regulate interactions between macromolecules. However, in the solid-state, these resonances are particularly difficult to resolve, even in relatively small proteins. We show that magic-angle-spinning (MAS) frequencies of 160 kHz, combined with a high magnetic field of 1200 MHz proton Larmor frequency, significantly improve their spectral...

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0 Replies | 266 Views
Biochemistry Seminar: Rachel Martin, “Protein aging and cataract ... - City University of New York
Oct 11, 2023 - 3:50 PM - by nmrlearner
nmrlearner's Avatar Biochemistry Seminar: Rachel Martin, “Protein aging and cataract ... - City University of New York

Biochemistry Seminar: Rachel Martin, “Protein aging and cataract ... City University of New York Read here
0 Replies | 231 Views
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