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231225s2018 xx |||||o 00| ||eng c |
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|a 10.1016/j.pnmrs.2018.06.002
|2 doi
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|a pubmed25n0971.xml
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|a (DE-627)NLM291574025
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|a (NLM)30527136
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|a (PII)S0079-6565(18)30012-8
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Demers, Jean-Philippe
|e verfasserin
|4 aut
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|a Structure determination of supra-molecular assemblies by solid-state NMR
|b Practical considerations
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|c 2018
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 12.02.2019
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|a Date Revised 15.02.2019
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2018 Elsevier B.V. All rights reserved.
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|a In the cellular environment, biomolecules assemble in large complexes which can act as molecular machines. Determining the structure of intact assemblies can reveal conformations and inter-molecular interactions that are only present in the context of the full assembly. Solid-state NMR (ssNMR) spectroscopy is a technique suitable for the study of samples with high molecular weight that allows the atomic structure determination of such large protein assemblies under nearly physiological conditions. This review provides a practical guide for the first steps of studying biological supra-molecular assemblies using ssNMR. The production of isotope-labeled samples is achievable via several means, which include recombinant expression, cell-free protein synthesis, extraction of assemblies directly from cells, or even the study of assemblies in whole cells in situ. Specialized isotope labeling schemes greatly facilitate the assignment of chemical shifts and the collection of structural data. Advanced strategies such as mixed, diluted, or segmental subunit labeling offer the possibility to study inter-molecular interfaces. Detailed and practical considerations are presented with respect to first setting up magic-angle spinning (MAS) ssNMR experiments, including the selection of the ssNMR rotor, different methods to best transfer the sample and prepare the rotor, as well as common and robust procedures for the calibration of the instrument. Diagnostic spectra to evaluate the resolution and sensitivity of the sample are presented. Possible improvements that can reduce sample heterogeneity and improve the quality of ssNMR spectra are reviewed
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Review
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|a Isotope labeling
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|a Protein expression
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|a Protein structure
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|a Solid-state Nuclear Magnetic Resonance
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|a Supra-molecular assembly
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|a Proteins
|2 NLM
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|a Fricke, Pascal
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Shi, Chaowei
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Chevelkov, Veniamin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Lange, Adam
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Progress in nuclear magnetic resonance spectroscopy
|d 1998
|g 109(2018) vom: 28. Dez., Seite 51-78
|w (DE-627)NLM098212745
|x 1873-3301
|7 nnns
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| 773 |
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|g volume:109
|g year:2018
|g day:28
|g month:12
|g pages:51-78
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|u http://dx.doi.org/10.1016/j.pnmrs.2018.06.002
|3 Volltext
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