Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution.
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New Insights from Sum Frequency Generation Vibrational Spectroscopy into the Interactions of Islet Amyloid Polypeptides with Lipid MembranesStructure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environmentSecondary Structure of Rat and Human Amylin across Force FieldsExploring the aggregation propensity of γS-crystallin protein variants using two-dimensional spectroscopic toolsMid-infrared spectroscopy for protein analysis: potential and challenges.Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.2D IR spectroscopy using four-wave mixing, pulse shaping, and IR upconversion: a quantitative comparison.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.Human islet amyloid polypeptide monomers form ordered beta-hairpins: a possible direct amyloidogenic precursor.Spectroscopic studies of protein folding: linear and nonlinear methodsSolution structures of rat amylin peptide: simulation, theory, and experiment.Molecular structures of quiescently grown and brain-derived polymorphic fibrils of the Alzheimer amyloid abeta9-40 peptide: a comparison to agitated fibrils.Probing the folding of mini-protein Beta3s by two-dimensional infrared spectroscopy; simulation study.Aromaticity and amyloid formation: effect of π-electron distribution and aryl substituent geometry on the self-assembly of peptides derived from hIAPP(22-29).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 two-dimensional infrared spectroscopy: quantitative analysis of protein secondary structure in solution.Polarized Raman Spectroscopy of Aligned Insulin FibrilsConformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation.Two-dimensional ultraviolet (2DUV) spectroscopic tools for identifying fibrillation propensity of protein residue sequencesStable and metastable states of human amylin in solution.Efficient microwave-assisted synthesis of human islet amyloid polypeptide designed to facilitate the specific incorporation of labeled amino acids.Residue-specific, real-time characterization of lag-phase species and fibril growth during amyloid formation: a combined fluorescence and IR study of p-cyanophenylalanine analogs of islet amyloid polypeptideResidue-specific fluorescent probes of α-synuclein: detection of early events at the N- and C-termini during fibril assemblyProbing amyloid fibril growth by two-dimensional near-ultraviolet spectroscopyTwo-dimensional near-ultraviolet spectroscopy of aromatic residues in amyloid fibrils: a first principles study.Mutational analysis of preamyloid intermediates: the role of his-tyr interactions in islet amyloid formationIntrinsic determinants of Aβ(12-24) pH-dependent self-assembly revealed by combined computational and experimental studies.Deep UV resonance Raman spectroscopy of β-sheet amyloid fibrils: a QM/MM simulation.Multidimensional infrared spectroscopy reveals the vibrational and solvation dynamics of isoniazid.Two-dimensional IR spectroscopy of protein dynamics using two vibrational labels: a site-specific genetically encoded unnatural amino acid and an active site ligandDetection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins.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.Thermally induced protein unfolding probed by isotope-edited IR spectroscopy.Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation.
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P2860
Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 03 April 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Two-dimensional IR spectroscop ...... h residue-specific resolution.
@en
Two-dimensional IR spectroscop ...... h residue-specific resolution.
@nl
type
label
Two-dimensional IR spectroscop ...... h residue-specific resolution.
@en
Two-dimensional IR spectroscop ...... h residue-specific resolution.
@nl
prefLabel
Two-dimensional IR spectroscop ...... h residue-specific resolution.
@en
Two-dimensional IR spectroscop ...... h residue-specific resolution.
@nl
P2093
P2860
P356
P1476
Two-dimensional IR spectroscop ...... h residue-specific resolution.
@en
P2093
David B Strasfeld
Martin T Zanni
Ruchi Gupta
Yun L Ling
P2860
P304
P356
10.1073/PNAS.0805957106
P407
P577
2009-04-03T00:00:00Z