Related ArticlesPositively-Charged Tags Impede Protein Mobility in Cells as Quantified by 19F NMR.
J Phys Chem B. 2019 May 01;:
Authors: Ye Y, Wu Q, Zheng W, Jiang B, Pielak GJ, Liu M, Li C
Abstract
Proteins are often tagged for visualization or delivery in the "sea" of other macromolecules in cells but how tags affect protein mobility remains poorly understood. Here, we employ 19F in-cell NMR to quantify the mobility of proteins with charged tags in Escherichia coli cells and Xenopus laevis oocytes. We find that the transient charge-charge interactions between the tag and cellular components affect protein mobility. More specifically, positively-charged tags impede protein mobility.
PMID: 31042382 [PubMed - as supplied by publisher]
[NMR paper] Quantification of size effect on protein rotational mobility in cells by 19F NMR spectroscopy.
Quantification of size effect on protein rotational mobility in cells by 19F NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Quantification of size effect on protein rotational mobility in cells by 19F NMR spectroscopy.
Anal Bioanal Chem. 2017 Nov 28;:
Authors: Ye Y, Wu Q, Zheng W, Jiang B, Pielak GJ, Liu M, Li C
Abstract
Protein diffusion in living cells might differ significantly from that measured in vitro. Little is known...
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12-01-2017 09:24 PM
A Soluble, Folded Protein without Charged Amino AcidResidues
A Soluble, Folded Protein without Charged Amino AcidResidues
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00269/20160628/images/medium/bi-2016-00269x_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00269
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/Gkdzui0Df1I
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07-07-2016 04:21 AM
[NMR paper] A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR.
A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR.
A Positively Charged Liquid Crystalline Medium for Measuring Residual Dipolar Couplings in Membrane Proteins by NMR.
J Am Chem Soc. 2015 Sep 8;
Authors: Thiagarajan-Rosenkranz Paltr Uic Edu P, Draney AW, Smrt ST, Lorieau JL
Abstract
Residual Dipolar Couplings (RDCs) are integral to the refinement of membrane protein structures by NMR since they accurately define the orientation of helices and other structural...
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09-09-2015 11:49 AM
[NMR paper] NMR spectroscopy of proteins encapsulated in a positively charged surfactant.
NMR spectroscopy of proteins encapsulated in a positively charged surfactant.
Related Articles NMR spectroscopy of proteins encapsulated in a positively charged surfactant.
J Magn Reson. 2005 Jul;175(1):158-62
Authors: Lefebvre BG, Liu W, Peterson RW, Valentine KG, Wand AJ
Traditionally, large proteins, aggregation-prone proteins, and membrane proteins have been difficult to examine by modern multinuclear and multidimensional solution NMR spectroscopy. A major limitation presented by these protein systems is that their slow molecular...
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11-25-2010 08:21 PM
[NMR paper] NMR study on the binding of d(GGAAATTTCC)2 with a positively charged pentacosapeptide
NMR study on the binding of d(GGAAATTTCC)2 with a positively charged pentacosapeptide.
Related Articles NMR study on the binding of d(GGAAATTTCC)2 with a positively charged pentacosapeptide.
Biochim Biophys Acta. 1998 Nov 8;1442(2-3):137-47
Authors: van Lieshout E, Hemminga MA
To obtain a better understanding of the electrostatic nature of protein-nucleic acid interactions, we have investigated the interaction of a double-stranded decamer d(GGAAATTTCC)2 with a synthetic arginine and lysine-rich pentacosapeptide (Pep25), using NMR and optical...
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11-17-2010 11:15 PM
Efficient protein production method for NMR using soluble protein tags with cold shoc
Efficient protein production method for NMR using soluble protein tags with cold shock expression vector
Abstract The E. coli protein expression system is one of the most useful methods employed for NMR sample preparation. However, the production of some recombinant proteins in E. coli is often hampered by difficulties such as low expression level and low solubility. To address these problems, a modified cold-shock expression system containing a glutathione S-transferase (GST) tag, the pCold-GST system, was investigated. The pCold-GST system successfully expressed 9 out of 10 proteins...
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09-18-2010 04:53 AM
[NMR paper] NMR analysis reveals a positively charged hydrophobic domain as a common motif to bou
NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Related Articles NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Biochemistry. 1994 Jan 25;33(3):644-50
Authors: Fraenkel Y, Gershoni JM, Navon G
A complete 1H assignment of d-tubocurarine was carried out using 1D and 2D NMR techniques. Geometries of free acetylcholine (ACh) and d-tubocurarine were compared with those of the ligands bound to a...
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08-22-2010 03:33 AM
[NMR paper] NMR analysis reveals a positively charged hydrophobic domain as a common motif to bou
NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Related Articles NMR analysis reveals a positively charged hydrophobic domain as a common motif to bound acetylcholine and d-tubocurarine.
Biochemistry. 1994 Jan 25;33(3):644-50
Authors: Fraenkel Y, Gershoni JM, Navon G
A complete 1H assignment of d-tubocurarine was carried out using 1D and 2D NMR techniques. Geometries of free acetylcholine (ACh) and d-tubocurarine were compared with those of the ligands bound to a...
Positively-Charged Tags Impede Protein Mobility in Cells as Quantified by 19F NMR.
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