Abstract
Understanding how the crowded and complex cellular milieu affects protein stability and dynamics has only recently become possible by using techniques such as in-cell nuclear magnetic resonance. However, the combination of stabilizing and destabilizing interactions makes simple predictions difficult. Here we show the potential of Danio rerio oocytes as an in-cell nuclear magnetic resonance model that can be widely used to measure protein stability and dynamics. We demonstrate that in eukaryotic oocytes, which are 3-6-fold less crowded than other cell types, attractive chemical interactions still dominate effects on protein stability and slow tumbling times, compared to the effects of dilute buffer.
PMID: 33534998 [PubMed - as supplied by publisher]
[NMR paper] A bioresistant nitroxide spin label for in-cell EPR spectroscopy: in vitro and in oocytes protein structural dynamics studies.
A bioresistant nitroxide spin label for in-cell EPR spectroscopy: in vitro and in oocytes protein structural dynamics studies.
Approaching proteins structural dynamics and protein-protein interactions in the cellular environment is a fundamental challenge. Due to its absolute sensitivity and to its selectivity to paramagnetic species, Site-Directed Spin Labeling (SDSL) combined with Electron Paramagnetic Resonance (EPR) has the potential to evolve into an efficient method to follow conformational changes in proteins directly inside cells. Until now, the use of nitroxyde-based spin labels...
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[NMR paper] (1)H NMR-based metabolomics analysis of adult zebrafish (Danio rerio) after exposure to diniconazole as well as its bioaccumulation behavior.
(1)H NMR-based metabolomics analysis of adult zebrafish (Danio rerio) after exposure to diniconazole as well as its bioaccumulation behavior.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles (1)H NMR-based metabolomics analysis of adult zebrafish (Danio rerio) after exposure to diniconazole as well as its bioaccumulation behavior.
Chemosphere. 2017 Feb;168:1571-1577
Authors: Wang Y, Zhu W, Wang D, Teng M, Yan J, Miao J, Zhou Z
Abstract
As a...
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[NMR paper] Bacterial cell wall composition and the influence of antibiotics by cell-wall and whole-cell NMR.
Bacterial cell wall composition and the influence of antibiotics by cell-wall and whole-cell NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-roysocjnls_full.gif Related Articles Bacterial cell wall composition and the influence of antibiotics by cell-wall and whole-cell NMR.
Philos Trans R Soc Lond B Biol Sci. 2015 Oct 5;370(1679)
Authors: Romaniuk JA, Cegelski L
Abstract
The ability to characterize bacterial cell-wall composition and structure is...
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07-07-2016 05:58 PM
[NMR paper] Frontispiece: Labeling Strategy and Signal Broadening Mechanism of Protein NMR Spectroscopy in Xenopus laevis Oocytes.
Frontispiece: Labeling Strategy and Signal Broadening Mechanism of Protein NMR Spectroscopy in Xenopus laevis Oocytes.
Related Articles Frontispiece: Labeling Strategy and Signal Broadening Mechanism of Protein NMR Spectroscopy in Xenopus laevis Oocytes.
Chemistry. 2015 Jun 8;21(24)
Authors: Ye Y, Liu X, Chen Y, Xu G, Wu Q, Zhang Z, Yao C, Liu M, Li C
Abstract
NMR Spectroscopy In their Communication on page 8686 ff., C. Li et al., demonstrate that (19) F labeling is a good first choice for studying globular and disordered...
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[NMR paper] Labeling Strategy and Signal Broadening Mechanism of Protein NMR Spectroscopy in Xenopus laevis Oocytes.
Labeling Strategy and Signal Broadening Mechanism of Protein NMR Spectroscopy in Xenopus laevis Oocytes.
Labeling Strategy and Signal Broadening Mechanism of Protein NMR Spectroscopy in Xenopus laevis Oocytes.
Chemistry. 2015 May 12;
Authors: Ye Y, Liu X, Chen Y, Xu G, Wu Q, Zhang Z, Yao C, Liu M, Li C
Abstract
We used Xenopus laevis oocytes, a paradigm for a variety of biological studies, as a eukaryotic model system for in-cell protein NMR spectroscopy. The small globular protein GB1 was one of the first studied in...
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[NMR paper] Direct Observation of Ca(2+) -Induced Calmodulin Conformational Transitions in Intact Xenopus laevis Oocytes by (19) F NMR Spectroscopy.
Direct Observation of Ca(2+) -Induced Calmodulin Conformational Transitions in Intact Xenopus laevis Oocytes by (19) F NMR Spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary_FullTextOnline_120x27.gif Related Articles Direct Observation of Ca(2+) -Induced Calmodulin Conformational Transitions in Intact Xenopus laevis Oocytes by (19) F NMR Spectroscopy.
Angew Chem Int Ed Engl. 2015 Mar 5;
Authors: Ye Y, Liu X, Xu G, Liu M, Li C
Abstract
The...
Danio rerio Oocytes for Eukaryotic In-Cell NMR.
Linear Mode
