Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.
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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 sequencesA 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 spectroscopyTwo-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 simulationsA peptide's perspective of water dynamicsDistinguishing 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-phenylalanineTracking the mechanism of fibril assembly by simulated two-dimensional ultraviolet spectroscopyEmpirical 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 fibrilsTwo-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 fibrilsStudy 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 spectroscopyStructural 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?
P2860
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P2860
Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.
@ast
Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.
@en
type
label
Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.
@ast
Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.
@en
prefLabel
Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.
@ast
Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.
@en
P2093
P2860
P356
P1476
Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.
@en
P2093
Paul H Axelsen
Robin M Hochstrasser
Yung Sam Kim
P2860
P304
P356
10.1073/PNAS.0802993105
P407
P577
2008-05-22T00:00:00Z