2D IR provides evidence for mobile water molecules in beta-amyloid fibrils - Wikidata - awgldk - TriplyDB

2D IR provides evidence for mobile water molecules in beta-amyloid fibrils

2D IR provides evidence for mobile water molecules in beta-amyloid fibrils

http://www.wikidata.org/entity/Q37394372

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Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wires Site-specific infrared probes of proteins Snapshot of the equilibrium dynamics of a drug bound to HIV-1 reverse transcriptase Computing infrared spectra of proteins using the exciton model Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Utilizing Lifetimes to Suppress Random Coil Features in 2D IR Spectra of Peptides.Residue-specific structural kinetics of proteins through the union of isotope labeling, mid-IR pulse shaping, and coherent 2D IR spectroscopy.2D IR spectra of cyanide in water investigated by molecular dynamics simulations.Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO)Spectroscopic studies of protein folding: linear and nonlinear methods Principles governing oligomer formation in amyloidogenic peptides.Hollow core of Alzheimer's Abeta42 amyloid observed by cryoEM is relevant at physiological pH.Discriminating early stage A{beta}42 monomer structures using chirality-induced 2DIR spectroscopy in a simulation study.Coherent two-dimensional infrared spectroscopy: quantitative analysis of protein secondary structure in solution.Separating instability from aggregation propensity in γS-crystallin variants.Protein dynamics in cytochrome P450 molecular recognition and substrate specificity using 2D IR vibrational echo spectroscopy.2D IR photon echo of azido-probes for biomolecular dynamics Tidal surge in the M2 proton channel, sensed by 2D IR spectroscopy.Perspective: Reaches of chemical physics in biology.2D IR spectroscopy of histidine: probing side-chain structure and dynamics via backbone amide vibrations.Myeloperoxidase-mediated Methionine Oxidation Promotes an Amyloidogenic Outcome for Apolipoprotein A-I.Role of water in protein aggregation and amyloid polymorphism.Vibrational spectroscopy of water in hydrated lipid multi-bilayers. II. Two-dimensional infrared and peak shift observables within different theoretical approximations Multidimensional infrared spectroscopy reveals the vibrational and solvation dynamics of isoniazid.Broadband two dimensional infrared spectroscopy of cyclic amide 2-Pyrrolidinone.Frequency distribution of the amide-I vibration sorted by residues in amyloid fibrils revealed by 2D-IR measurements and simulations A peptide's perspective of water dynamics Site-specific hydration dynamics of globular proteins and the role of constrained water in solvent exchange with amphiphilic cosolvents.Parallel β-sheet vibrational couplings revealed by 2D IR spectroscopy of an isotopically labeled macrocycle: quantitative benchmark for the interpretation of amyloid and protein infrared spectra.Intrinsic structural heterogeneity and long-term maturation of amyloid β peptide fibrils Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet.Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage Inconvenient facts about pathological amyloid fibrils.Not All β-Sheets Are the Same: Amyloid Infrared Spectra, Transition Dipole Strengths, and Couplings Investigated by 2D IR Spectroscopy.2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure.Transient 2D-IR spectroscopy of inorganic excited states.The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation.Distinguishing gramicidin D conformers through two-dimensional infrared spectroscopy of vibrational excitons.Instantaneous ion configurations in the K+ ion channel selectivity filter revealed by 2D IR spectroscopy.Probing the Effects of Gating on the Ion Occupancy of the K+ Channel Selectivity Filter Using Two-Dimensional Infrared Spectroscopy

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2D IR provides evidence for mobile water molecules in beta-amyloid fibrils

http://www.wikidata.org/entity/Q37394372

description

article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 08 October 2009

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

@cs

name

2D IR provides evidence for mobile water molecules in beta-amyloid fibrils

@en

2D IR provides evidence for mobile water molecules in beta-amyloid fibrils.

@nl

type

label

2D IR provides evidence for mobile water molecules in beta-amyloid fibrils

@en

2D IR provides evidence for mobile water molecules in beta-amyloid fibrils.

@nl

prefLabel

2D IR provides evidence for mobile water molecules in beta-amyloid fibrils

@en

2D IR provides evidence for mobile water molecules in beta-amyloid fibrils.

@nl

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PNAS.0909888106

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Proceedings of the National Academy of Sciences of the United States of America

P1476

2D IR provides evidence for mobile water molecules in beta-amyloid fibrils

@en

P2093

Liu Liu

http://www.w3.org/2001/XMLSchema#string

Paul H Axelsen

http://www.w3.org/2001/XMLSchema#string

Robin M Hochstrasser

http://www.w3.org/2001/XMLSchema#string

Yung Sam Kim

http://www.w3.org/2001/XMLSchema#string

P2860

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils

Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange

Structure and dynamics of parallel beta-sheets, hydrophobic core, and loops in Alzheimer's A beta fibrils

3D structure of Alzheimer's amyloid-beta(1-42) fibrils

Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils

Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.

Molecular dynamics simulations of Alzheimer's beta-amyloid protofilaments.

Polymorphic fibril formation by residues 10-40 of the Alzheimer's beta-amyloid peptide.

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17751-17756

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scholarly article

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10.1073/PNAS.0909888106

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42

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106

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2009-10-08T00:00:00Z

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19815514

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2764887

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