Protein interactions in the Escherichia coli cytosol: an impediment to in-cell NMR spectroscopy. - Wikidata - awgldk - TriplyDB

Protein interactions in the Escherichia coli cytosol: an impediment to in-cell NMR spectroscopy.

Protein interactions in the Escherichia coli cytosol: an impediment to in-cell NMR spectroscopy.

http://www.wikidata.org/entity/Q30401276

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Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Protein camouflage in cytochrome c-calixarene complexes Silica as a matrix for encapsulating proteins: surface effects on protein structure assessed by circular dichroism spectroscopy.Quinary structure modulates protein stability in cells.A cell is more than the sum of its (dilute) parts: A brief history of quinary structure.Is buffer a good proxy for a crowded cell-like environment? A comparative NMR study of calmodulin side-chain dynamics in buffer and E. coli lysate Protein dynamics in living cells studied by in-cell NMR spectroscopy.(19) F NMR spectroscopy as a probe of cytoplasmic viscosity and weak protein interactions in living cells.Soft interactions and crowding.Residue level quantification of protein stability in living cells.Exploring weak, transient protein--protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy.The transcriptional repressor domain of Gli3 is intrinsically disordered Recent advances in protein NMR spectroscopy and their implications in protein therapeutics research.Specific ion effects on macromolecular interactions in Escherichia coli extracts.Changes in apparent molar water volume and DKP solubility yield insights on the Hofmeister effect.Protein interaction patterns in different cellular environments are revealed by in-cell NMR.A Unique Tool for Cellular Structural Biology: In-cell NMR.Impact of reconstituted cytosol on protein stability.Computer Simulations of the Bacterial Cytoplasm.In-cell NMR and EPR spectroscopy of biomacromolecules.Study of cytochrome c-DNA interaction--evaluation of binding sites on the redox protein.Grasping the nature of the cell interior: from Physiological Chemistry to Chemical Biology.In-cell NMR: a topical review Functional binding surface of a β-hairpin VEGF receptor targeting peptide determined by NMR spectroscopy in living cells.Protein folding, binding, and droplet formation in cell-like conditions.Cosolute and Crowding Effects on a Side-By-Side Protein Dimer.Hydrogen exchange of disordered proteins in Escherichia coli.Transient Interactions of a Cytosolic Protein with Macromolecular and Vesicular Cosolutes: Unspecific and Specific Effects.Intracellular pH modulates quinary structure.Selective observation of the disordered import signal of a globular protein by in-cell NMR: the example of frataxins.How crowded is the prokaryotic cytoplasm?Ribosome surface properties may impose limits on the nature of the cytoplasmic proteome.Quantitative Determination of Interacting Protein Surfaces in Prokaryotes and Eukaryotes by Using In-Cell NMR Spectroscopy.Quinary interactions with an unfolded state ensemble.Ribosome Mediated Quinary Interactions Modulate In-Cell Protein Activities.In-cell NMR: from metabolites to macromolecules.Direct observation of Ca(2+) -induced calmodulin conformational transitions in intact Xenopus laevis oocytes by (19) F NMR spectroscopy.Protein charge determination and implications for interactions in cell extracts.Interaction proteomics by using in-cell NMR spectroscopy.Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies.

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P2860

Protein interactions in the Escherichia coli cytosol: an impediment to in-cell NMR spectroscopy.

http://www.wikidata.org/entity/Q30401276

description

2011 nî lūn-bûn

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2011 թուականի Մարտին հրատարակուած գիտական յօդուած

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Protein interactions in the Es ...... t to in-cell NMR spectroscopy.

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Protein interactions in the Es ...... t to in-cell NMR spectroscopy.

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Protein interactions in the Es ...... t to in-cell NMR spectroscopy.

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Protein interactions in the Es ...... t to in-cell NMR spectroscopy.

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Protein interactions in the Es ...... t to in-cell NMR spectroscopy.

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Protein interactions in the Es ...... t to in-cell NMR spectroscopy.

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Protein interactions in the Es ...... nt to in-cell NMR spectroscopy

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Elysian Chow

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Tatiana Papkovskaia

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P2860

Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences

Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c

Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR

Dynamic docking of cytochrome b5 with myoglobin and alpha-hemoglobin: heme-neutralization "squares" and the binding of electron-transfer-reactive configurations

Regulation of protein function: crystal packing interfaces and conformational dimerization

Protein structure determination in living cells by in-cell NMR spectroscopy

High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c

Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c550 and cytochrome cd1 nitrite reductase

Three-dimensional solution structure of Saccharomyces cerevisiae reduced iso-1-cytochrome c

Protein production by auto-induction in high density shaking cultures

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1043-1048

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scholarly article

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10.1002/CBIC.201100063

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7

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12

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Peter B. Crowley

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2011-03-29T00:00:00Z

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50908355

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21448871

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Escherichia coli