Amyloid fibrils are large and insoluble protein assemblies composed of a rigid core associated with a cross-? arrangement rich in ?-sheet structural elements. It has been widely observed in solid-state NMR experiments that semi-rigid protein segments or side chains do not yield easily observable NMR signals at room temperature. The reasons for the missing peaks may be due to the presence of unfavorable dynamics that interfere with NMR experiments, which result in very weak or unobservable NMR...
[NMR paper] Linear discriminant analysis reveals hidden patterns in NMR chemical shifts of intrinsically disordered proteins
Linear discriminant analysis reveals hidden patterns in NMR chemical shifts of intrinsically disordered proteins
NMR spectroscopy is key in the study of intrinsically disordered proteins (IDPs). Yet, even the first step in such an analysis-the assignment of observed resonances to particular nuclei-is often problematic due to low peak dispersion in the spectra of IDPs. We show that the assignment process can be aided by finding "hidden" chemical shift patterns specific to the amino acid residue types. We find such patterns in the training data from the Biological Magnetic Resonance Bank...
nmrlearner
Journal club
0
10-07-2022 08:36 AM
[NMR paper] Dynamics of Serine-8 Side-Chain in Amyloid-? Fibrils and Fluorenylmethyloxycarbonyl Serine Amino Acid, Investigated by Solid-State Deuteron NMR.
Dynamics of Serine-8 Side-Chain in Amyloid-? Fibrils and Fluorenylmethyloxycarbonyl Serine Amino Acid, Investigated by Solid-State Deuteron NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Dynamics of Serine-8 Side-Chain in Amyloid-? Fibrils and Fluorenylmethyloxycarbonyl Serine Amino Acid, Investigated by Solid-State Deuteron NMR.
J Phys Chem B. 2020 May 12;:
Authors: Vugmeyster L, Au DF, Ostrovsky D, Rickertsen DRL, Reed SM
Abstract
Serine...
nmrlearner
Journal club
0
05-13-2020 09:14 PM
[NMR paper] Solvent-Driven Dynamical Cross-Over in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected by (2)H NMR Relaxation.
Solvent-Driven Dynamical Cross-Over in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected by (2)H NMR Relaxation.
Related Articles Solvent-Driven Dynamical Cross-Over in the Phenylalanine Side-Chain from the Hydrophobic Core of Amyloid Fibrils Detected by (2)H NMR Relaxation.
J Phys Chem B. 2017 Jul 12;:
Authors: Vugmeyster L, Ostrovsky D, Hoatson GL, Qiang W, Falconer IB
Abstract
Aromatic residues are important markers of dynamical changes in proteins' hydrophobic cores. In this work we...
nmrlearner
Journal club
0
07-13-2017 12:02 PM
Amyloid-like Fibrils from an ?-HelicalTransmembrane Protein
Amyloid-like Fibrils from an ?-HelicalTransmembrane Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00157/20170612/images/medium/bi-2017-00157c_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00157
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/1BmLUgzNxlY
More...
nmrlearner
Journal club
0
06-13-2017 06:55 AM
[NMR paper] NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils.
NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils.
NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils.
Angew Chem Int Ed Engl. 2016 Nov 16;:
Authors: Stanek J, Andreas LB, Jaudzems K, Cala D, Lalli D, Bertarello A, Schubeis T, Akopjana I, Kotelovica S, Tars K, Pica A, Leone S, Picone D, Xu ZQ, Dixon NE, Martinez D, Berbon M, El Mammeri N, Noubhani...
nmrlearner
Journal club
0
11-20-2016 09:20 PM
[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] Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
Related Articles Solid-state NMR study reveals Collagen I structural modifications of amino-acid side chains upon fibrillogenesis.
J Biol Chem. 2013 Jan 22;
Authors: De Sa Peixoto P, Laurent G, Azais T, Mosser G
Abstract
In vivo, collagen I, the major structural protein in human body, is found assembled into fibrils. In the present work, we study a high concentrated collagen sample in its soluble, fibrillar and denatured states...
nmrlearner
Journal club
0
02-03-2013 10:19 AM
[Question from NMRWiki Q&A forum] selecting for side chains
selecting for side chains
Does anyone know of literature pointing to NMR experiments that can select for say -CH3 groups attached to -CH2?
Check if somebody has answered this question on NMRWiki QA forum
Efficient 18.8*T MAS-DNP NMR reveals hidden side chains in amyloid fibrils
Linear Mode
