Related ArticlesQuantitative Determination of Interacting Protein Surfaces in Prokaryotes and Eukaryotes by Using In-Cell NMR Spectroscopy.
Methods Mol Biol. 2018;1688:423-444
Authors: Burz DS, DeMott CM, Aldousary A, Dansereau S, Shekhtman A
Abstract
This paper describes three protocols for identifying interacting surfaces on (15)N-labeled target proteins of known structure by using in-cell NMR spectroscopy. The first protocol describes how to identify protein quinary structure interaction surfaces in prokaryotes by using cross-relaxation-induced polarization transfer, CRIPT, based in-cell NMR. The second protocol describes how to introduce labeled protein into eukaryotic (HeLa) cells via electroporation for CRIPT-based in-cell studies. The third protocol describes how to quantitatively map protein interacting surfaces by utilizing singular value decomposition, SVD, analysis of STructural INTeractions by in-cell NMR, STINT-NMR, data.
[NMR paper] Quantitative determination and validation of octreotide acetate using (1) H-NMR spectroscopy with internal standard method.
Quantitative determination and validation of octreotide acetate using (1) H-NMR spectroscopy with internal standard method.
Related Articles Quantitative determination and validation of octreotide acetate using (1) H-NMR spectroscopy with internal standard method.
Magn Reson Chem. 2017 Sep 15;:
Authors: Yu C, Zhang Q, Xu PY, Bai Y, Shen WB, Di B, Su MX
Abstract
Quantitative nuclear magnetic resonance (qNMR) is a well-established technique in quantitative analysis. We presented a validated (1) H quantitative nuclear magnetic...
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09-19-2017 04:40 PM
ReAsH as a Quantitative Probe of In-Cell Protein Dynamics
ReAsH as a Quantitative Probe of In-Cell Protein Dynamics
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01336/20160317/images/medium/bi-2015-013367_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01336
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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03-18-2016 05:23 PM
Understanding macromolecular crowding is critical for quantitative cell biology - SPIE Newsroom
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Understanding macromolecular crowding is critical for quantitative cell biology
SPIE Newsroom
In the past, nuclear magnetic resonance (NMR) has been used to study protein-crowded environments and to investigate the translational and rotational diffusion of chymotrypsin inhibitor 2 in crowded environments. It was found that the heterogeneity of ...
Understanding macromolecular crowding is critical for...
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12-12-2015 03:39 AM
[NMR paper] NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains.
NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains.
Related Articles NMR mapping of RANTES surfaces interacting with CCR5 using linked extracellular domains.
FEBS J. 2013 Mar 8;
Authors: Schnur E, Kessler N, Zherdev Y, Noah E, Scherf T, Ding FX, Rabinovich S, Arshava B, Kurbatska V, Leonciks A, Tsimanis A, Rosen O, Naider F, Anglister J
Abstract
Chemokines constitute a large family of small proteins that regulate leukocyte trafficking to the site of inflammation by binding to specific cell-surface...
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03-14-2013 10:05 PM
[NMR paper] Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR.
Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR.
Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR.
Chem Commun (Camb). 2013 Feb 26;
Authors: Takaoka Y, Kioi Y, Morito A, Otani J, Arita K, Ashihara E, Ariyoshi M, Tochio H, Shirakawa M, Hamachi I
Abstract
Here we describe how a (19)F-probe incorporated into an endogenous protein by a chemical biology method revealed protein dynamics. By explicit determination of ligand-bound and unbound structures with...
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02-27-2013 06:47 PM
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
J Agric Food Chem. 2011 Jan 10;
Authors: Monogioudi E, Permi P, Filpponen I, Lienemann M, Li B, Argyropoulos D, Buchert J, Mattinen ML
Cross-linking of ?-casein by Trichoderma reesei tyrosinase (TrTyr) and Streptoverticillium mobaraense transglutaminase (Tgase) was analyzed by (31)P nuclear magnetic...
Quantitative Determination of Interacting Protein Surfaces in Prokaryotes and Eukaryotes by Using In-Cell NMR Spectroscopy.
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