Related ArticlesQuenched hydrogen-deuterium exchange NMR of a disease-relevant A?(1-42) amyloid polymorph.
PLoS One. 2017;12(3):e0172862
Authors: Wälti MA, Orts J, Riek R
Abstract
Alzheimer's disease is associated with the aggregation into amyloid fibrils of A?(1-42) and A?(1-40) peptides. Interestingly, these fibrils often do not obtain one single structure but rather show different morphologies, so-called polymorphs. Here, we compare quenched hydrogen-deuterium (H/D) exchange of a disease-relevant A?(1-42) fibril for which the 3D structure has been determined by solid-state NMR with H/D exchange previously determined on another structural polymorph. This comparison reveals secondary structural differences between the two polymorphs suggesting that the two polymorphisms can be classified as segmental polymorphs.
[NMR paper] Quenched Hydrogen Exchange NMR of Amyloid Fibrils.
Quenched Hydrogen Exchange NMR of Amyloid Fibrils.
Related Articles Quenched Hydrogen Exchange NMR of Amyloid Fibrils.
Methods Mol Biol. 2016;1345:211-22
Authors: Alexandrescu AT
Abstract
Amyloid fibrils are associated with a number of human diseases. These aggregatively misfolded intermolecular ?-sheet assemblies constitute some of the most challenging targets in structural biology because to their complexity, size, and insolubility. Here, protocols and controls are described for experiments designed to study hydrogen-bonding in...
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10-12-2015 01:04 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
[NMR paper] NMR-Based Detection of Hydrogen/Deuterium Exchange in Liposome-Embedded Membrane Proteins.
NMR-Based Detection of Hydrogen/Deuterium Exchange in Liposome-Embedded Membrane Proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png Related Articles NMR-Based Detection of Hydrogen/Deuterium Exchange in Liposome-Embedded Membrane Proteins.
PLoS One. 2014;9(11):e112374
Authors: Yao X, Dürr UH, Gattin Z, Laukat Y, Narayanan RL, Brückner AK, Meisinger C, Lange A, Becker S, Zweckstetter M
Abstract
Membrane proteins play key roles in biology. Determination of...
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11-08-2014 12:08 AM
[NMR paper] Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR.
Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR.
PLoS One. 2013;8(2):e56467
Authors: Alexandrescu AT
Abstract
Amylin is an endocrine hormone that...
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08-29-2013 01:53 PM
[NMR paper] An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed
An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A.
Related Articles An NMR-based quenched hydrogen exchange investigation of model amyloid fibrils formed by cold shock protein A.
Pac Symp Biocomput. 2001;:67-78
Authors: Alexandrescu AT
Acid-denatured cold shock protein A (CspA) self-assembles into polymers with properties typical of amyloid fibrils. In the present work, a quenched hydrogen exchange experiment was used to probe the interactions of CspA fibrils with solvent. Exchange...
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11-19-2010 08:32 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] Mechanism of hydrogen-deuterium exchange in trp repressor studied by 1H-15N NMR.
Mechanism of hydrogen-deuterium exchange in trp repressor studied by 1H-15N NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Mechanism of hydrogen-deuterium exchange in trp repressor studied by 1H-15N NMR.
J Mol Biol. 1995 Nov 3;253(4):576-89
Authors: Finucane MD, Jardetzky O
Amide proton exchange rates have been measured for fast-exchanging amides in trp aporepressor, and compared with the rates measured in the holorepressor. The results indicate that the presence...
Quenched hydrogen-deuterium exchange NMR of a disease-relevant A?(1-42) amyloid polymorph.
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