Alzheimer's disease (AD) is classified as an amyloid-related disease. Amyloid beta (A?) is a transmembrane protein known to play a major role in the pathogenesis of AD. These A? proteins can form ion channels or pores in the cell membrane. Studies have elucidated the structure of the transmembrane domain of A? ion channels. In addition, various studies have investigated substances that block or inhibit the formation of A? ion channels. Zinc ions are considered as potential inhibitors of AD. In...
[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...
nmrlearner
Journal club
0
03-07-2021 07:38 AM
[NMR paper] NMR localization of the O-mycoloylation on PorH, a channel forming peptide from Corynebacterium glutamicum.
NMR localization of the O-mycoloylation on PorH, a channel forming peptide from Corynebacterium glutamicum.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR localization of the O-mycoloylation on PorH, a channel forming peptide from Corynebacterium glutamicum.
FEBS Lett. 2013 Nov 15;587(22):3687-91
Authors: Rath P, Saurel O, Tropis M, Daffé M, Demange P, Milon A
Abstract
PorH and PorA are two small peptides that, in complex, form a...
nmrlearner
Journal club
0
01-08-2014 11:23 AM
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
From The DNP-NMR Blog:
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
Lopez Del Amo, J.M., et al., Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP. J Biomol NMR, 2013: p. 1-5.
http://www.ncbi.nlm.nih.gov/pubmed/23793606
nmrlearner
News from NMR blogs
0
08-14-2013 05:24 PM
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
From The DNP-NMR Blog:
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-beta peptide: perspectives for DNP
Lopez del Amo, J.-M., et al., Cryogenic solid state NMR studies of fibrils of the Alzheimer’s disease amyloid-? peptide: perspectives for DNP. J. Biomol. NMR, 2013: p. 1-5.
http://www.ncbi.nlm.nih.gov/pubmed/23793606
[NMR paper] Channel-forming membrane permeabilization by an antibacterial protein, sapecin: deter
Channel-forming membrane permeabilization by an antibacterial protein, sapecin: determination of membrane-buried and oligomerization surfaces by NMR.
Related Articles Channel-forming membrane permeabilization by an antibacterial protein, sapecin: determination of membrane-buried and oligomerization surfaces by NMR.
J Biol Chem. 2004 Feb 6;279(6):4981-7
Authors: Takeuchi K, Takahashi H, Sugai M, Iwai H, Kohno T, Sekimizu K, Natori S, Shimada I
The action mechanism of sapecin, an antibacterial peptide with membrane permeabilization activity, was...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Conformational changes of colicin Ia channel-forming domain upon membrane binding: a
Conformational changes of colicin Ia channel-forming domain upon membrane binding: a solid-state NMR study.
Related Articles Conformational changes of colicin Ia channel-forming domain upon membrane binding: a solid-state NMR study.
Biochim Biophys Acta. 2002 Apr 12;1561(2):159-70
Authors: Huster D, Yao X, Jakes K, Hong M
Channel-forming colicins are bactericidal proteins that spontaneously insert into hydrophobic lipid bilayers. We have used magic-angle spinning solid-state nuclear magnetic resonance spectroscopy to examine the conformational...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] 1H NMR studies on the interaction of beta-carboline derivatives with human serum albu
1H NMR studies on the interaction of beta-carboline derivatives with human serum albumin.
Related Articles 1H NMR studies on the interaction of beta-carboline derivatives with human serum albumin.
J Magn Reson. 1998 Feb;130(2):281-6
Authors: Veglia G, Delfini M, Giudice MR, Gaggelli E, Valensin G
1H NMR studies were performed on two beta-carboline derivatives interacting with human serum albumin. The spin-lattice relaxation rates of the two derivatives, having side chains of different length and polarity, were used to demonstrate a diverse...
NMR Studies of the Ion Channel-Forming Human Amyloid-beta with Zinc Ion Concentrations
Linear Mode
