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Protein Trends & Technologies Market Research Report 2019 Analysis and Forecast To 2024 - The Daily Chronicle
Aug 05, 2020 - 12:48 PM - by nmrlearner
nmrlearner's Avatar Protein Trends & Technologies Market Research Report 2019 Analysis and Forecast To 2024 The Daily Chronicle
Protein Trends & Technologies Market Research Report 2019 Analysis and Forecast To 2024 - The Daily Chronicle
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0 Replies | 1 Views
Protein Crystallization Market, Share, Application Analysis, Regional Outlook, Competitive Strategies & Forecast up to 2026 - Bulletin Line
Aug 05, 2020 - 12:48 PM - by nmrlearner
nmrlearner's Avatar Protein Crystallization Market, Share, Application Analysis, Regional Outlook, Competitive Strategies & Forecast up to 2026 - Bulletin Line

Protein Crystallization Market, Share, Application Analysis, Regional Outlook, Competitive Strategies & Forecast up to 2026 Bulletin Line Read here
0 Replies | 1 Views
[ASAP] Resilient Intracrystalline Occlusions: A Solid-State NMR View of Local Structure as It Tunes Bulk Lattice Properties
Aug 04, 2020 - 12:56 PM - by nmrlearner
nmrlearner's Avatar [ASAP] Resilient Intracrystalline Occlusions: A Solid-State NMR View of Local Structure as It Tunes Bulk Lattice Properties

Ira Ben Shir†, Shifi Kababya†, David B. Zax‡, and Asher Schmidt*†



Journal of the American Chemical Society
DOI: 10.1021/jacs.0c03590



Source: Journal of the American Chemical Society
0 Replies | 14 Views
[NMR paper] NMR characterization of the C-mannose conformation in a thrombospondin repeat using a selective labeling approach.
Aug 04, 2020 - 12:56 PM - by nmrlearner
nmrlearner's Avatar NMR characterization of the C-mannose conformation in a thrombospondin repeat using a selective labeling approach.

NMR characterization of the C-mannose conformation in a thrombospondin repeat using a selective labeling approach.

Angew Chem Int Ed Engl. 2020 Aug 03;:

Authors: Jonker HRA, Saxena K, Shcherbakova A, Tiemann B, Bakker H, Schwalbe H

Abstract
Despite the great interest in glycoproteins, structural information reporting on conformation and dynamics of the sugar moieties are limited. We present a new biochemical method to express proteins with glycans that are selectively labeled with NMR active nuclei. We report on the incorporation of 13C-labeled mannose in the C-mannosylated UNC-5 thrombospondin repeat. The conformational landscape of the C-mannose sugar puckers attached to tryptophan residues of UNC-5 is characterized by interconversion between the canonical 1C4 state and the B03 / 1S3 state. This flexibility may be essential for protein folding and stabilization. We foresee that this versatile tool to produce proteins with selective labeled C-mannose can be applied and adjusted to other systems and modifications and potentially paves a way to advance glycoprotein research by unravelling the dynamical and conformational properties of glycan structures and their interactions.


PMID: 32745319 [PubMed - as supplied by publisher]



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[NMR paper] Refolding of cold denatured barstar induced by radio frequency heating - new method to study protein folding by real-time NMR spectroscopy.
Aug 04, 2020 - 12:56 PM - by nmrlearner
nmrlearner's Avatar Refolding of cold denatured barstar induced by radio frequency heating - new method to study protein folding by real-time NMR spectroscopy.

Related Articles Refolding of cold denatured barstar induced by radio frequency heating - new method to study protein folding by real-time NMR spectroscopy.

Angew Chem Int Ed Engl. 2020 Aug 03;:

Authors: Pintér G, Schwalbe H

Abstract
The C40A/C82A double mutant of barstar has been shown to undergo cold denaturation above the water freezing point. By rapidly applying radio frequency power to lossy aqueous samples, refolding of barstar from its cold denatured state can be followed by real-time NMR spectroscopy. Since temperature-induced unfolding and refolding is reversible for this double mutant, multiple cycling can be utilized to obtain 2D real-time NMR data. Barstar contains two proline residues that adopt a mix of cis and trans conformations in the low temperature-unfolded state, which can potentially induce multiple folding pathways. The high time resolution real-time 2D-NMR measurements reported here show evidence for multiple folding pathways related to proline isomerization, and stable intermediates are populated. By application of advanced heating cycles and state-correlated spectroscopy, an alternative folding pathway circumventing the rate limiting cis-trans isomerization could be observed. The kinetic data revealed intermediates on both, the... [Read More]
0 Replies | 5 Views
[NMR paper] Enabling NMR studies of high molecular weight systems without the need for deuteration: The XL-ALSOFAST experiment with delayed decoupling.
Aug 04, 2020 - 12:56 PM - by nmrlearner
nmrlearner's Avatar Enabling NMR studies of high molecular weight systems without the need for deuteration: The XL-ALSOFAST experiment with delayed decoupling.

Related Articles Enabling NMR studies of high molecular weight systems without the need for deuteration: The XL-ALSOFAST experiment with delayed decoupling.

Angew Chem Int Ed Engl. 2020 Aug 03;:

Authors: Rößler P, Mathieu D, Gossert AD

Abstract
Current biological research increasingly focusses on large human proteins and their complexes. Such proteins are difficult to study by NMR spectroscopy because they often can only be produced in higher eukaryotic expression systems, where deuteration is hardly feasible. Here, we present the XL-ALSOFAST-[ 13 C, 1 H]-HMQC experiment with much improved sensitivity for fully protonated high-molecular weight proteins. For the tested systems ranging from 100 to 240*kDa in size, 3-fold higher sensitivity was obtained on average for fast relaxing signals compared to current state-of-the-art experiments. In the XL-ALSOFAST approach, non-observed magnetisation is optimally exploited and transverse relaxation is minimized by the newly introduced concept of delayed decoupling. The combination of high sensitivity and superior artefact suppression makes it ideal for studying inherently unstable membrane proteins or for analysing therapeutic antibodies at natural 13 C abundance. The XL-ALSOFAST and delayed decoupling will... [Read More]
0 Replies | 6 Views
[NMR paper] Structure and dynamics of a nanodisc by integrating NMR, SAXS and SANS experiments with molecular dynamics simulations.
Aug 01, 2020 - 2:01 PM - by nmrlearner
nmrlearner's Avatar Structure and dynamics of a nanodisc by integrating NMR, SAXS and SANS experiments with molecular dynamics simulations.

Related Articles Structure and dynamics of a nanodisc by integrating NMR, SAXS and SANS experiments with molecular dynamics simulations.

Elife. 2020 Jul 30;9:

Authors: Bengtsen T, Holm VL, Kjølbye LR, Midtgaard SR, Johansen NT, Tesei G, Bottaro S, Schiøtt B, Arleth L, Lindorff-Larsen K

Abstract
Nanodiscs are membrane mimetics that consist of a protein belt surrounding a lipid bilayer, and are broadly used for characterization of membrane proteins. Here, we investigate the structure, dynamics and biophysical properties of two small nanodiscs, MSP1D1?H5 and ?H4H5. We combine our SAXS and SANS experiments with molecular dynamics simulations and previously obtained NMR and EPR data to derive and validate a conformational ensemble that represents the structure and dynamics of the nanodisc. We find that it displays conformational heterogeneity with various elliptical shapes, and with substantial differences in lipid ordering in the centre and rim of the... [Read More]
0 Replies | 12 Views
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