Quo Vadis Biomolecular NMR Spectroscopy?

Selenko, Philipp

doi:10.3390/ijms20061278

Cited by 20 publications

(17 citation statements)

References 199 publications

(220 reference statements)

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“…Certain IDPs, including αS, are relatively more prone to aggregation than globular proteins. It is possible that αS represents one of those IDPs for which carrying out an NMR structural investigation should be performed with much more precaution than one might think, e.g., under a well-controlled condition resembling the native cellular settings as much as possible [109]. Certain sample conditions could modulate IDP conformations as exemplified here for the αS protein.…”

Section: Discussionmentioning

confidence: 99%

Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy

et al. 2020

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Elucidating the structural details of proteins is highly valuable and important for the proper understanding of protein function. In the case of intrinsically disordered proteins (IDPs), however, obtaining the structural details is quite challenging, as the traditional structural biology tools have only limited use. Nuclear magnetic resonance (NMR) is a unique experimental tool that provides ensemble conformations of IDPs at atomic resolution, and when studying IDPs, a slightly different experimental strategy needs to be employed than the one used for globular proteins. We address this point by reviewing many NMR investigations carried out on the α-synuclein protein, the aggregation of which is strongly correlated with Parkinson’s disease.

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Section: Discussionmentioning

confidence: 99%

Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy

et al. 2020

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“…3. Technically, MP EUTs are pluggable and should be plugged an experimental data-driven hybrid approach [60][61][62][63][64][65][66][67][68][69][70][71][72][73]. In other words, the continued development of PDB with less and less MP EUTs within is within the reach of currently available tools, experimental and computational.…”

Section: Conclusion and Discussionmentioning

confidence: 99%

Visualising the Experimentally Uncharted Territories of Membrane Protein Structures inside Protein Data Bank

Li¹

2020

Preprint

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As of today, there is not any direct report yet of the degree to which missing residues exist for experimentally determined membrane protein (MP) structures, which constitute more than half of current drug targets. With a chain- and position-specific visualisation and a statistical analysis of all MP structures inside PDB (as of September 25, 2019), this article argues that the experimentally uncharted territories (EUTs, i.e., consisting of missing residues) within PDB are pluggable and should be plugged with an experimental data-driven hybrid approach, and calls for continued development of MP structural determination with less and less EUTs, in light of MPs' crucial role in biological and biomedical research, both fundamental and pharmaceutical.

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“…Unlike other analytical tools, solution state NMR spectroscopy is non-destructive and enables high resolution monitoring of dynamic changes of biomolecules, including metabolites 16 , proteins 17 and nucleic acids 18 in a tag-free manner and in complex environments that range from cell extracts to whole cells. In particular, NMR metabolomics has emerged as a powerful tool to characterize the metabolic compositions of such complex samples, including animal tissue extracts or body fluids and their response to environmental or genetic conditions that result in metabolic changes [19][20][21][22][23] .…”

Section: Introductionmentioning

confidence: 99%

Unsaturated fatty acids profiling in liveC. elegansusing real-time NMR spectroscopy

Prez

et al. 2021

Preprint

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Unsaturated fatty acids (UFAs) impact central cellular process in animals such as membrane function, development and disease. Perturbations of UFAs homeostasis contribute to the onset of metabolic, cardiovascular and neurodegenerative disorders. Nevertheless, links between lipid desaturation fluctuations and the dynamics of mono and polyunsaturated fatty acid synthesis in live animal physiology are poorly understood. To advance in the understanding of this process, we decided to study de novo UFAs synthesis with the highest resolution possible in live Caenorhabditis elegans. Conventional lipid analysis in this organism involves solvent extraction procedures coupled with analytical techniques such as chromatography and/or mass spectrometry. These methodologies are destructive and prevent the access of information, linking in vivo UFA dynamics and functionality. To overcome these limitations, we used uniform 13C isotope labeling and real-time 2D heteronuclear NMR spectroscopy in live C. elegans to identify their UFA compositions and the dynamic response of these fatty acids during cold adaptation. Our methodology allowed us to monitor in real time the upregulation of UFA synthesis when ambient temperature is decreased. The analysis of UFAs synthesis in worms lacking the adiponectin receptor AdipoR2 homolog PAQR-2 during a temperature drop supports the pivotal role of this protein in low temperature adaptation and survival. Our results provide new insights about the environmental regulation of UFAs and establish methodological benchmarks for future investigations of fatty acid regulation under experimental conditions that recapitulate human diseases.

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Quo Vadis Biomolecular NMR Spectroscopy?

Cited by 20 publications

References 199 publications

Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy

Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy

Visualising the Experimentally Uncharted Territories of Membrane Protein Structures inside Protein Data Bank

Unsaturated fatty acids profiling in liveC. elegansusing real-time NMR spectroscopy

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