Hydrogen/Deuterium Exchange Mass Spectrometry of HumanGreen Opsin Reveals a Conserved Pro-Pro Motif in Extracellular Loop2 of Monostable Visual G Protein-Coupled Receptors
Hydrogen/Deuterium Exchange Mass Spectrometry of HumanGreen Opsin Reveals a Conserved Pro-Pro Motif in Extracellular Loop2 of Monostable Visual G Protein-Coupled Receptors
[NMR paper] Partially unfolded forms of the prion protein populated under misfolding-promoting conditions: characterization by hydrogen exchange mass spectrometry and NMR.
Partially unfolded forms of the prion protein populated under misfolding-promoting conditions: characterization by hydrogen exchange mass spectrometry and NMR.
Partially unfolded forms of the prion protein populated under misfolding-promoting conditions: characterization by hydrogen exchange mass spectrometry and NMR.
J Biol Chem. 2015 Aug 25;
Authors: Moulick R, Das R, Udgaonkar JB
Abstract
The susceptibility of the cellular prion protein (PrP(C)) to convert to an alternative misfolded conformation (PrP(Sc)), which is the key...
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08-26-2015 10:21 AM
[NMR paper] [Interactions between proteins and cation exchange adsorbents analyzed by NMR and hydrogen/deuterium exchange technique].
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Sheng Wu Gong Cheng Xue Bao. 2014 Sep;30(9):1454-63
Authors: Wang K, Hao D, Qi S, Ma G
Abstract
In silico acquirement of the accurate residue details of protein on chromatographic media is a bottleneck in protein chromatography separation and purification. Here we developed a novel approach by coupling with H/D exchange and nuclear magnetic resonance to observe hen egg white lysozyme (HEWL) unfolding behavior adsorbed on cation exchange media (SP Sepharose FF). Analysis of 1D 1H-NMR shows that protein unfolding accelerated...
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03-01-2015 12:18 PM
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein.
Biophys J. 2011 Aug 3;101(3):L23-L25
Authors: Wang S, Shi L, Kawamura I, Brown LS, Ladizhansky V
Solid-state NMR spectroscopy is an efficient tool for following conformational dynamics of membrane proteins at atomic resolution. We used this technique for the site-specific...
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08-03-2011 12:00 PM
Interactions between CusF and CusB Identified by NMR Spectroscopy and Chemical Cross-Linking Coupled to Mass Spectrometry
Interactions between CusF and CusB Identified by NMR Spectroscopy and Chemical Cross-Linking Coupled to Mass Spectrometry
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi102012j/aop/images/medium/bi-2010-02012j_0006.gif
Biochemistry
DOI: 10.1021/bi102012j
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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03-09-2011 04:19 AM
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry.
Biochemistry. 2011 Feb 16;
Authors: Mealman TD, Bagai I, Singh P, Goodlet DR, Rensing C, Zhou H, Wysocki VH, McEvoy MM
The E. coli periplasmic proteins CusF and CusB, as part of the CusCFBA efflux system, aid in the resistance of elevated levels of copper and silver by direct metal transfer between the...
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02-18-2011 08:07 PM
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state N
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy
Abstract We present the quantification of backbone amide hydrogen-deuterium exchange rates (HDX) for immobilized proteins. The experiments make use of the deuterium isotope effect on the amide nitrogen chemical shift, as well as on proton dilution by deuteration. We find that backbone amides in the microcrystalline α-spectrin SH3 domain exchange rather slowly with the solvent (with exchange rates negligible within the individual 15Nâ??T 1 timescales). We observed chemical exchange for 6...
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10-27-2010 08:51 AM
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state N
Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy.
Related Articles Quantification of protein backbone hydrogen-deuterium exchange rates by solid state NMR spectroscopy.
J Biomol NMR. 2010 Oct 20;
Authors: Del Amo JM, Fink U, Reif B
We present the quantification of backbone amide hydrogen-deuterium exchange rates (HDX) for immobilized proteins. The experiments make use of the deuterium isotope effect on the amide nitrogen chemical shift, as well as on proton dilution by deuteration. We find that...
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10-22-2010 06:02 AM
[NMR paper] Solid-state NMR studies of the mechanism of the opsin shift in the visual pigment rho
Solid-state NMR studies of the mechanism of the opsin shift in the visual pigment rhodopsin.
Related Articles Solid-state NMR studies of the mechanism of the opsin shift in the visual pigment rhodopsin.
Biochemistry. 1990 Sep 4;29(35):8158-64
Authors: Smith SO, Palings I, Miley ME, Courtin J, de Groot H, Lugtenburg J, Mathies RA, Griffin RG
Solid-state 13C NMR spectra have been obtained of bovine rhodopsin and isorhodopsin regenerated with retinal selectively 13C labeled along the polyene chain. In rhodopsin, the chemical shifts for 13C-5,...
Hydrogen/Deuterium Exchange Mass Spectrometry of HumanGreen Opsin Reveals a Conserved Pro-Pro Motif in Extracellular Loop2 of Monostable Visual G Protein-Coupled Receptors
Linear Mode
