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[NMR paper] Toward protein NMR at physiological concentrations by hyperpolarized water-Finding and mapping uncharted conformational spaces
Aug 06, 2022 - 7:25 AM - by nmrlearner
nmrlearner's Avatar Toward protein NMR at physiological concentrations by hyperpolarized water-Finding and mapping uncharted conformational spaces

Nuclear magnetic resonance (NMR) spectroscopy is a key method for determining the structural dynamics of proteins in their native solution state. However, the low sensitivity of NMR typically necessitates nonphysiologically high sample concentrations, which often limit the relevance of the recorded data. We show how to use hyperpolarized water by dissolution dynamic nuclear polarization (DDNP) to acquire protein spectra at concentrations of 1 ?M within seconds and with a high signal-to-noise...

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0 Replies | 20 Views
[NMR paper] SAA fibrils involved in AA amyloidosis are similar in bulk and by single particle reconstitution: A MAS solid-state NMR study
Aug 05, 2022 - 3:43 AM - by nmrlearner
nmrlearner's Avatar SAA fibrils involved in AA amyloidosis are similar in bulk and by single particle reconstitution: A MAS solid-state NMR study

AA amyloidosis is one of the most prevalent forms of systemic amyloidosis and affects both humans and other vertebrates. In this study, we compare MAS solid-state NMR data with a recent cryo-EM study of fibrils involving full-length murine SAA1.1. We address the question whether the specific requirements for the reconstitution of an amyloid fibril structure by cryo-EM can potentially yield a bias towards a particular fibril polymorph. We employ fibril seeds extracted from in to vivo material to...

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0 Replies | 34 Views
[NMR paper] The measurement of binding affinities by NMR chemical shift perturbation
Aug 04, 2022 - 1:03 AM - by nmrlearner
nmrlearner's Avatar The measurement of binding affinities by NMR chemical shift perturbation

We have carried out chemical shift perturbation titrations on three contrasting proteins. The resulting chemical shifts have been analysed to determine the best way to fit the data, and it is concluded that a simultaneous fitting of all raw shift data to a single dissociation constant is both the most accurate and the most precise method. It is shown that the optimal weighting of ^(15)N chemical shifts to ¹H chemical shifts is protein dependent, but is around the consensus value of 0.14. We show...

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0 Replies | 33 Views
[NMR paper] 15N-Detected TROSY NMR experiments to study large disordered proteins in high-field magnets
Aug 04, 2022 - 1:03 AM - by nmrlearner
nmrlearner's Avatar 15N-Detected TROSY NMR experiments to study large disordered proteins in high-field magnets

Intrinsically disordered regions (IDRs) of proteins are critical in the regulation of biological processes but difficult to study structurally. Nuclear magnetic resonance (NMR) is uniquely equipped to provide structural information on IDRs at atomic resolution; however, existing NMR methods often pose a challenge for large molecular weight IDRs. Resonance assignment of IDRs using ^(15)N^(D)-detection was previously demonstrated and shown to overcome some of these limitations. Here, we improve...

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0 Replies | 29 Views
[NMR paper] Aligned peptoid-based macrodiscs for structural studies of membrane proteins by oriented-sample nmr
Aug 04, 2022 - 1:03 AM - by nmrlearner
nmrlearner's Avatar ALIGNED PEPTOID-BASED MACRODISCS FOR STRUCTURAL STUDIES OF MEMBRANE PROTEINS BY ORIENTED-SAMPLE NMR

Development of a robust, uniform, and magnetically orientable lipid mimetics will undoubtedly advance solid-state NMR of macroscopically aligned membrane proteins. Here we report on a novel lipid membrane mimetic based on peptoid belts. The peptoids composed of 15 residues were synthesized by alternating N-(2-carboxyethyl)glycine with N-(2-phenethyl)glycine residues at the 2:1 molar ratio. The chemically synthesized peptoids possess much lower degree of polydispersity as compared to...

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0 Replies | 23 Views
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