Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40. - Wikidata - wikimedia - TriplyDB

Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.

Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.

http://www.wikidata.org/entity/Q36693949

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Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Recent progress in understanding Alzheimer's β-amyloid structures.Mid-infrared spectroscopy for protein analysis: potential and challenges.Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Three-dimensional structures by two-dimensional vibrational 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.How to turn your pump-probe instrument into a multidimensional spectrometer: 2D IR and Vis spectroscopies via pulse shaping.2D IR spectra of cyanide in water investigated by molecular dynamics simulations.Coherent multidimensional vibrational spectroscopy of biomolecules: concepts, simulations, and challenges.Simulation of two-dimensional ultraviolet spectroscopy of amyloid fibrils.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Discriminating early stage A{beta}42 monomer structures using chirality-induced 2DIR spectroscopy in a simulation study.Coherent multidimensional optical spectroscopy of excitons in molecular aggregates; quasiparticle versus supermolecule perspectives.Surface effects mediate self-assembly of amyloid-β peptides.Two-dimensional ultraviolet (2DUV) spectroscopic tools for identifying fibrillation propensity of protein residue sequences A synchrotron-based hydroxyl radical footprinting analysis of amyloid fibrils and prefibrillar intermediates with residue-specific resolution.Tidal surge in the M2 proton channel, sensed by 2D IR spectroscopy.Probing amyloid fibril growth by two-dimensional near-ultraviolet spectroscopy Two-dimensional near-ultraviolet spectroscopy of aromatic residues in amyloid fibrils: a first principles study.Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils.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 Distinguishing amyloid fibril structures in Alzheimer's disease (AD) by two-dimensional ultraviolet (2DUV) spectroscopy.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.Kinetic Isotope Effect Provides Insight into the Vibrational Relaxation Mechanism of Aromatic Molecules: Application to Cyano-phenylalanine Tracking the mechanism of fibril assembly by simulated two-dimensional ultraviolet spectroscopy Empirical amide I vibrational frequency map: application to 2D-IR line shapes for isotope-edited membrane peptide bundles.Intrinsic structural heterogeneity and long-term maturation of amyloid β peptide fibrils Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution.A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides.Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet.Two-dimensional stimulated resonance Raman spectroscopy study of the Trp-cage peptide folding.2D IR provides evidence for mobile water molecules in beta-amyloid fibrils Study of the γD-crystallin protein using two-dimensional infrared (2DIR) spectroscopy: experiment and simulation.Site-specific orientation of an α-helical peptide ovispirin-1 from isotope-labeled SFG spectroscopy Structural motif of polyglutamine amyloid fibrils discerned with mixed-isotope infrared spectroscopy.Identification of arginine residues in peptides by 2D-IR echo spectroscopy.Not All β-Sheets Are the Same: Amyloid Infrared Spectra, Transition Dipole Strengths, and Couplings Investigated by 2D IR Spectroscopy.A role for helical intermediates in amyloid formation by natively unfolded polypeptides?

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P2860

Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.

http://www.wikidata.org/entity/Q36693949

description

2008 nî lūn-bûn

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Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.

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Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.

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Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.

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Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.

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Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.

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Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.

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Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.

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Liu Liu

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Paul H Axelsen

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Robin M Hochstrasser

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Yung Sam Kim

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P2860

Electrostatics of nanosystems: application to microtubules and the ribosome

Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance.

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

Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils

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

Automated 2D IR spectroscopy using a mid-IR pulse shaper and application of this technology to the human islet amyloid polypeptide

The two-dimensional IR nonlinear spectroscopy of a cyclic penta-peptide in relation to its three-dimensional structure.

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infrared spectroscopy

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