Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy. - Wikidata - awgldk - TriplyDB

Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy.

Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy.

http://www.wikidata.org/entity/Q35532059

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Computing infrared spectra of proteins using the exciton model Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Three-dimensional structures by two-dimensional vibrational spectroscopy.Fully absorptive 3D IR spectroscopy using a dual mid-infrared pulse shaper.2D IR spectroscopy using four-wave mixing, pulse shaping, and IR upconversion: a quantitative comparison.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.Polarization shaping in the mid-IR and polarization-based balanced heterodyne detection with application to 2D IR spectroscopy.Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO)Solution structures of rat amylin peptide: simulation, theory, and experiment.Simulation of two-dimensional ultraviolet spectroscopy of amyloid fibrils.Surface effects mediate self-assembly of amyloid-β peptides.Time-resolved multiple probe spectroscopy.Two-dimensional ultraviolet (2DUV) spectroscopic tools for identifying fibrillation propensity of protein residue sequences Probing amyloid fibril growth by two-dimensional near-ultraviolet spectroscopy Mutational analysis of preamyloid intermediates: the role of his-tyr interactions in islet amyloid formation Distinguishing amyloid fibril structures in Alzheimer's disease (AD) by two-dimensional ultraviolet (2DUV) spectroscopy.Thermally induced protein unfolding probed by isotope-edited IR spectroscopy.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.Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution.Study of the γD-crystallin protein using two-dimensional infrared (2DIR) spectroscopy: experiment and simulation.Experimental implementations of 2D IR spectroscopy through a horizontal pulse shaper design and a focal plane array detector.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.Application of two-dimensional infrared spectroscopy to benchmark models for the amide I band of proteins.Inhibition of human amylin fibril formation by insulin-mimetic vanadium complexes.Ultrafast UV spectroscopy: from a local to a global view of dynamical processes in macromolecules.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.Applications of 2D IR spectroscopy to peptides, proteins, and hydrogen-bond dynamics Line shape analysis of two-dimensional infrared spectra Ester to amide switch peptides provide a simple method for preparing monomeric islet amyloid polypeptide under physiologically relevant conditions and facilitate investigations of amyloid formation Development and validation of transferable amide I vibrational frequency maps for peptides.Deamidation accelerates amyloid formation and alters amylin fiber structure Strategies for extracting structural information from 2D IR spectroscopy of amyloid: application to islet amyloid polypeptide.Effect of dehydration on the aggregation kinetics of two amyloid peptides.Residue-specific vibrational echoes yield 3D structures of a transmembrane helix dimer.Sulfoxide stretching mode as a structural reporter via dual-frequency two-dimensional infrared spectroscopy.Two-dimensional infrared study of 3-azidopyridine as a potential spectroscopic reporter of protonation state.Two-dimensional infrared spectroscopy provides evidence of an intermediate in the membrane-catalyzed assembly of diabetic amyloid.

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P2860

Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy.

http://www.wikidata.org/entity/Q35532059

description

2008 nî lūn-bûn

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2008 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2008 թվականի մայիսին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Tracking fiber formation in hu ...... automated 2D-IR spectroscopy.

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Tracking fiber formation in hu ...... automated 2D-IR spectroscopy.

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type

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Tracking fiber formation in hu ...... automated 2D-IR spectroscopy.

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Tracking fiber formation in hu ...... automated 2D-IR spectroscopy.

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Tracking fiber formation in hu ...... automated 2D-IR spectroscopy.

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Journal of the American Chemical Society

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Tracking fiber formation in hu ...... automated 2D-IR spectroscopy.

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P2093

David B Strasfeld

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Martin T Zanni

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Sang-Hee Shim

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Yun L Ling

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P2860

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

Two-dimensional infrared spectroscopy of antiparallel beta-sheet secondary structure.

Unfolding the role of protein misfolding in neurodegenerative diseases.

Simulation of two-dimensional infrared spectroscopy of amyloid fibrils.

Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR.

Lipid membranes modulate the structure of islet amyloid polypeptide.

Experimental evidence for the reorganization of beta-strands within aggregates of the Abeta(16-22) peptide.

Characteristic two-dimensional IR spectroscopic features of antiparallel and parallel beta-sheet polypeptides: simulation studies.

Conserved and Cooperative Assembly of Membrane-Bound α-Helical States of Islet Amyloid Polypeptide†

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10.1021/JA801483N

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21

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2008-05-07T00:00:00Z

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