[NMR paper] Dynamics of Serine-8 Side-Chain in Amyloid-? Fibrils and Fluorenylmethyloxycarbonyl Serine Amino Acid, Investigated by Solid-State Deuteron NMR.
Related ArticlesDynamics 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 side-chains are strategic sites of post-translational modifications and it is important to establish benchmarks of their internal dynamics. In this work we compare the dynamics of serine side-chains in several biologically important systems: Serine-8 in the disordered domain of A?(1-40) fibrils in the hydrated and dry states and fluorenylmethyloxycarbonyl(Fmoc) serine with the bulky group that mimics hydrophobicity of the fibrils contacts yet lacks the complexity of the protein system. Using deuterium solid-state NMR static line shape and longitudinal relaxation techniques in the 310 to 180 K temperature range, we compare the main features of the dynamics in these systems. The main motional modes in the fibrils are large-scale fluctuations in the hydrated state of the fibrils, as well as local motions such as 3-site jumps of the C?deuterons at high temperatures and small-angle fluctuations of the C?-C? axis at low temperatures. In the hydrated fibrils two distinct states are present with vastly different extent of large scale diffusive motions and 3-site jumps rate constants. The hydrated state at the physiological conditions is dominated by the "free" state undergoing large-scale diffusive motions and very fast local 3-site jumps, while in the "bound" state these large scale motions are quenched due to transient inter- and intra-molecular interactions. Additionally, in the bound state the 3-site jumps motions are orders of magnitude slower. Details of the dynamics in the serine side-chain are dependent on fine structural features and hydration levels of the systems.
PMID: 32396356 [PubMed - as supplied by publisher]
[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...
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WaterDistribution, Dynamics, and Interactions withAlzheimer’s ?-Amyloid Fibrils Investigated bySolid-State NMR
WaterDistribution, Dynamics, and Interactions withAlzheimer’s ?-Amyloid Fibrils Investigated bySolid-State NMR
Tuo Wang, Hyunil Jo, William F. DeGrado and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.7b02089/20170421/images/medium/ja-2017-02089e_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.7b02089
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/UN3-dx0SQ1I
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[NMR paper] Water Distribution, Dynamics and Interactions with Alzheimer's ?-Amyloid Fibrils Investigated by Solid-State NMR.
Water Distribution, Dynamics and Interactions with Alzheimer's ?-Amyloid Fibrils Investigated by Solid-State NMR.
Water Distribution, Dynamics and Interactions with Alzheimer's ?-Amyloid Fibrils Investigated by Solid-State NMR.
J Am Chem Soc. 2017 Apr 13;:
Authors: Wang T, Jo H, DeGrado WF, Hong M
Abstract
Water is essential for protein folding and assembly of amyloid fibrils. Internal water cavities have been proposed for several amyloid fibrils, but no direct structural and dynamical data have been reported on the water...
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04-14-2017 10:27 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...
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[NMR paper] Solution NMR structure and inhibitory effect against amyloid-? fibrillation of Humanin containing a D-isomerized serine residue.
Solution NMR structure and inhibitory effect against amyloid-? fibrillation of Humanin containing a D-isomerized serine residue.
Related Articles Solution NMR structure and inhibitory effect against amyloid-? fibrillation of Humanin containing a D-isomerized serine residue.
Biochem Biophys Res Commun. 2016 Jun 24;
Authors: Alsanousi N, Sugiki T, Furuita K, So M, Lee YH, Fujiwara T, Kojima C
Abstract
Humanin comprising 24 amino acid residues is a bioactive peptide that has been isolated from the brain tissue of patients with...
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Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Magn Reson Chem. 2011 Feb;49(2):65-9
Authors: Middleton DA
Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the...
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01-22-2011 01:52 PM
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14)N--(13)C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Magn Reson Chem. 2011 Jan 3;
Authors: Middleton DA
Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the secondary...
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01-05-2011 09:51 PM
Automated amino acid side-chain NMR assignment of proteins using 13C- and 15N-resolved 3D [1H,1H]-NOESY
Automated amino acid side-chain NMR assignment of proteins using 13C- and 15N-resolved 3D -NOESY
Francesco Fiorito, Torsten Herrmann, Fred F. Damberger and Kurt Wüthrich
Journal of Biomolecular NMR; 2008; 42(1); pp 23-33
Abstract
ASCAN is a new algorithm for automatic sequence-specific NMR assignment of amino acid side-chains in proteins, which uses as input the primary structure of the protein, chemical shift lists of 1HN, 15N, 13Cα, 13Cβ and possibly 1Hα from the previous polypeptide backbone assignment, and one or several 3D 13C- or 15N-resolved -NOESY spectra. ASCAN has also been...
Dynamics of Serine-8 Side-Chain in Amyloid-? Fibrils and Fluorenylmethyloxycarbonyl Serine Amino Acid, Investigated by Solid-State Deuteron NMR.
Linear Mode
