Related ArticlesQuenched 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 amyloid fibrils indirectly, by transferring information about amide proton occupancy in the fibrils to the dimethyl sulfoxide-denatured state. Since the denatured state is amenable to solution NMR spectroscopy, the method can provide residue-level-resolution data on hydrogen exchange for the monomers that make up the fibrils.
[NMR paper] Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_final.gif Related Articles Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid ?-fibrils in a redox cycle.
J Biol Chem. 2014 Apr 4;289(14):9998-10010
Authors: Parthasarathy S, Yoo B, McElheny D, Tay W,...
nmrlearner
Journal club
0
05-31-2014 01:57 PM
[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...
nmrlearner
Journal club
0
08-29-2013 01:53 PM
[NMR paper] The H/D-exchange Kinetics of the Escherichia coli Co-chaperonin GroES Studied by 2D-NMR and DMSO-Quenched Exchange Methods.
The H/D-exchange Kinetics of the Escherichia coli Co-chaperonin GroES Studied by 2D-NMR and DMSO-Quenched Exchange Methods.
Related Articles The H/D-exchange Kinetics of the Escherichia coli Co-chaperonin GroES Studied by 2D-NMR and DMSO-Quenched Exchange Methods.
J Mol Biol. 2013 Apr 11;
Authors: Chandak MS, Nakamura T, Makabe K, Takenaka T, Mukaiyama A, Chaudhuri TK, Kato K, Kuwajima K
Abstract
We studied hydrogen/deuterium-exchange reactions of peptide amide protons of GroES using two different techniques: (1) two-dimensional (1)H-(15)N...
nmrlearner
Journal club
0
04-16-2013 07:46 PM
[NMR paper] Hydrogen bonding in Alzheimer's amyloid-? fibrils probed by 15N{17O} REAPDOR solid-state NMR spectroscopy.
Hydrogen bonding in Alzheimer's amyloid-? fibrils probed by 15N{17O} REAPDOR solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Hydrogen bonding in Alzheimer's amyloid-? fibrils probed by 15N{17O} REAPDOR solid-state NMR spectroscopy.
Angew Chem Int Ed Engl. 2012 Oct 8;51(41):10289-92
Authors: Antzutkin ON, Iuga D, Filippov AV, Kelly RT, Becker-Baldus J, Brown SP, Dupree R
PMID: 22976560
nmrlearner
Journal club
0
02-16-2013 08:00 PM
The use of spin desalting columns in DMSO-quenched H/D-exchange NMR experiments
The use of spin desalting columns in DMSO-quenched H/D-exchange NMR experiments
Abstract
Dimethylsulfoxide (DMSO)-quenched hydrogen/deuterium (H/D)-exchange is a powerful method to characterize the H/D-exchange behaviors of proteins and protein assemblies, and it is potentially useful for investigating non-protected fast-exchanging amide protons in the unfolded state. However, the method has not been used for studies on fully unfolded proteins in a concentrated denaturant or protein solutions at high salt concentrations. In all of the current DMSO-quenched H/D-exchange studies of...
nmrlearner
Journal club
0
02-11-2013 08:42 AM
[NMR paper] The use of spin desalting columns in DMSO-quenched H/D-exchange NMR experiments.
The use of spin desalting columns in DMSO-quenched H/D-exchange NMR experiments.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles The use of spin desalting columns in DMSO-quenched H/D-exchange NMR experiments.
Protein Sci. 2013 Jan 22;
Authors: Chandak MS, Nakamura T, Takenaka T, Chaudhuri TK, Yagi-Utsumi M, Chen J, Kato K, Kuwajima K
Abstract
DMSO-quenched H/D-exchange is a powerful method to characterize the H/D-exchange behaviors of...
nmrlearner
Journal club
0
02-03-2013 10:19 AM
The use of spin desalting columns in DMSO-quenched H/D-exchange NMR experiments
The use of spin desalting columns in DMSO-quenched H/D-exchange NMR experiments
Abstract
DMSO-quenched H/D-exchange is a powerful method to characterize the H/D-exchange behaviors of proteins and protein assemblies, and it is potentially useful for investigating non-protected fast-exchanging amide protons in the unfolded state. However, the method has not been used for studies on fully unfolded proteins in a concentrated denaturant or protein solutions at high salt concentrations. In all of the current DMSO-quenched H/D-exchange studies of proteins so far reported, lyophilization was...
nmrlearner
Journal club
0
02-03-2013 09:54 AM
[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...