The amount of bonds between constituting parts of a protein aggregate were determined in wild type (WT) and A53T ?-synuclein (?S) oligomers, amyloids and in the complex of thymosin-?(4)-cytoplasmic domain of stabilin-2 (T?(4)-stabilin CTD). A53T ?S aggregates have more extensive ?sheet contents reflected by constant regions at low potential barriers in difference (to monomers) melting diagrams (MDs). Energies of the intermolecular interactions and of secondary structures bonds, formed during...
[NMR paper] Structural details of amyloid beta oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy
Structural details of amyloid beta oligomers in complex with human prion protein as revealed by solid-state MAS NMR spectroscopy
Human PrP (huPrP) is a high-affinity receptor for oligomeric amyloid-? (A?) protein aggregates. Binding of A? oligomers to membrane-anchored huPrP has been suggested to trigger neurotoxic cell signaling in Alzheimer's disease, while an N-terminal soluble fragment of huPrP can sequester A? oligomers and reduce their toxicity. Synthetic oligomeric A? species are known to be heterogeneous, dynamic and transient, rendering their structural investigation particularly...
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03-07-2021 07:38 AM
[ASAP] Protein Modifications Critical for Myonectin/Erythroferrone Secretion and Oligomer Assembly
Protein Modifications Critical for Myonectin/Erythroferrone Secretion and Oligomer Assembly
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00461/20200706/images/medium/bi0c00461_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00461
http://feeds.feedburner.com/~r/acs/bichaw/~4/yEPI8223n_0
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07-08-2020 03:03 AM
[NMR paper] Protein-Solvent Interfaces in Human Y145Stop Prion Protein Amyloid Fibrils Probed by Paramagnetic Solid-State NMR Spectroscopy.
Protein-Solvent Interfaces in Human Y145Stop Prion Protein Amyloid Fibrils Probed by Paramagnetic Solid-State NMR Spectroscopy.
Related Articles Protein-Solvent Interfaces in Human Y145Stop Prion Protein Amyloid Fibrils Probed by Paramagnetic Solid-State NMR Spectroscopy.
J Struct Biol. 2018 Apr 18;:
Authors: Aucoin D, Xia Y, Theint T, Nadaud PS, Surewicz K, Surewicz WK, Jaroniec CP
Abstract
The C-terminally truncated Y145Stop variant of prion protein (PrP23-144), which is associated with heritable PrP cerebral amyloid angiopathy...
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04-22-2018 10:46 PM
[NMR paper] Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.
Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.
Related Articles Wide-line NMR and DSC studies on intrinsically disordered p53 transactivation domain and its helically pre-structured segment.
BMB Rep. 2016 Apr 4;
Authors: Tompa P, Kim KH, Bokor M, Kamasa P, Tantos Á, Fritz B, Kim DH, Lee C, Verebélyi T, Tompa K
Abstract
Wide-line 1H NMR intensity and differential scanning calorimetry measurements were carried out on the intrinsically disordered...
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07-16-2016 10:22 PM
[NMR paper] The "long tail" of the protein tumbling correlation function: observation by (1)H NMR relaxometry in a wide frequency and concentration range.
The "long tail" of the protein tumbling correlation function: observation by (1)H NMR relaxometry in a wide frequency and concentration range.
Related Articles The "long tail" of the protein tumbling correlation function: observation by (1)H NMR relaxometry in a wide frequency and concentration range.
J Biomol NMR. 2015 Nov 18;
Authors: Roos M, Hofmann M, Link S, Ott M, Balbach J, Rössler E, Saalwächter K, Krushelnitsky A
Abstract
Inter-protein interactions in solution affect the auto-correlation function of Brownian tumbling not...
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11-20-2015 06:29 PM
The â??long tailâ?? of the protein tumbling correlation function: observation by 1 H NMR relaxometry in a wide frequency and concentration range
The â??long tailâ?? of the protein tumbling correlation function: observation by 1 H NMR relaxometry in a wide frequency and concentration range
Abstract
Inter-protein interactions in solution affect the auto-correlation function of Brownian tumbling not only in terms of a simple increase of the correlation time, they also lead to the appearance of a weak slow component (â??long tailâ??) of the correlation function due to a slowly changing local anisotropy of the microenvironment. The conventional protocol of correlation time estimation from the...
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11-19-2015 05:22 PM
Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry - Nature.com
Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry - Nature.com
http://www.bionmr.com//t2.gstatic.com/images?q=tbn:ANd9GcSCXR38-W1skwr6nJyTpI7ekwp0MTCyjWVm3-nHyO5fN0ai5Hxu348VoeOV77NUFQBjMN6RfXbk
Nature.com
<img alt="" height="1" width="1">
Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry
Nature.com
We describe an integrated workflow that robustly identifies cross-links from endogenous protein complexes in human cellular lysates. Our approach is based on the application of mass spectrometry (MS)-cleavable cross-linkers,...
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09-29-2015 07:59 AM
[Question from NMRWiki Q&A forum] How to extract residue information in case of line broadening (intensity drop ) of HSQC titration of protein - protein interaction data ?
How to extract residue information in case of line broadening (intensity drop ) of HSQC titration of protein - protein interaction data ?
Dear Friends
we have done HSQC gradient titration with targeted proteins , most of cross peaks we observed intensity drop , 30 out of 95 peaks ( 70 percent intensity drop of each cross peak ) , other cross peaks also we observe intensity drop less than 70 percent , we did n"t observe any chemical shift change .( May be it is due to intermediate exchange regime of complex ) .ITC experiment showing 12uM binding constant .AUC experiment result is...
Protein-Protein Connections-Oligomer, Amyloid and Protein Complex-By Wide Line (1)H NMR
Linear Mode
