Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils. - Wikidata - wikimedia - TriplyDB

Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils.

Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils.

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Site-specific infrared probes of proteins Assessment of amide I spectroscopic maps for a gas-phase peptide using IR-UV double-resonance spectroscopy and density functional theory calculations Spatially Resolved Two-Dimensional Infrared Spectroscopy via Wide-Field Microscopy Mid-infrared spectroscopy for protein analysis: potential and challenges.Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.Comparative analysis of human γD-crystallin aggregation under physiological and low pH conditions.Myeloperoxidase-mediated Methionine Oxidation Promotes an Amyloidogenic Outcome for Apolipoprotein A-I.The βγ-crystallins: native state stability and pathways to aggregation.Applications of two-dimensional infrared spectroscopy Thermally induced protein unfolding probed by isotope-edited IR 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.Protein misfolding and aggregation in cataract disease and prospects for prevention.A strongly absorbing class of non-natural labels for probing protein electrostatics and solvation with FTIR and 2D IR spectroscopies.Meandering Down the Energy Landscape of Protein Folding: Are We There Yet?Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage Study of the γD-crystallin protein using two-dimensional infrared (2DIR) spectroscopy: experiment and simulation.Tyrosine/cysteine cluster sensitizing human γD-crystallin to ultraviolet radiation-induced photoaggregation in vitro.Structural motif of polyglutamine amyloid fibrils discerned with mixed-isotope infrared spectroscopy.Not All β-Sheets Are the Same: Amyloid Infrared Spectra, Transition Dipole Strengths, and Couplings Investigated by 2D IR Spectroscopy.A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin.Stability and cytotoxicity of crystallin amyloid nanofibrils.Application of two-dimensional infrared spectroscopy to benchmark models for the amide I band of proteins.Deamidation accelerates amyloid formation and alters amylin fiber structure An alternative structural isoform in amyloid-like aggregates formed from thermally denatured human γD-crystallin.Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor Evidence for Intramolecular Antiparallel Beta-Sheet Structure in Alpha-Synuclein Fibrils from a Combination of Two-Dimensional Infrared Spectroscopy and Atomic Force Microscopy.How to Get Insight into Amyloid Structure and Formation from Infrared Spectroscopy.General strategy for the bioorthogonal incorporation of strongly absorbing, solvation-sensitive infrared probes into proteins.Identifying Cu(ii)-amyloid peptide binding intermediates in the early stages of aggregation by resonance Raman spectroscopy: a simulation study.A molecular engineering toolbox for the structural biologist.Ultrafast structural molecular dynamics investigated with 2D infrared spectroscopy methods.Segmental Deuteration of α-Synuclein for Neutron Reflectometry on Tethered Bilayers.Protection of human γB-crystallin from UV-induced damage by epigallocatechin gallate: spectroscopic and docking studies.Amyloid β-Sheet Secondary Structure Identified in UV-Induced Cataracts of Porcine Lenses using 2D IR Spectroscopy.Investigation of the early stages of human γD-crystallin aggregation process.Couplings between hierarchical conformational dynamics from multi-time correlation functions and two-dimensional lifetime spectra: Application to adenylate kinase.Ultrafast vibrational and structural dynamics of dimeric cyclopentadienyliron dicarbonyl examined by infrared spectroscopy.Isotope-Labeled Amyloids via Synthesis, Expression, and Chemical Ligation for Use in FTIR, 2D IR, and NMR Studies.

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P2860

Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils.

http://www.wikidata.org/entity/Q35807714

description

2012 nî lūn-bûn

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name

Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.

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Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.

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type

label

Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.

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Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.

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Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.

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Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.

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

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Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.

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Ann Marie Woys

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Eli Bixby

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Lauren E Buchanan

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Martin T Zanni

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Sean D Moran

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Sean M Decatur

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P2860

Structure of the cross-beta spine of amyloid-like fibrils

High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract

Synthesis of proteins by native chemical ligation

Expressed protein ligation (EPL) in the study of signal transduction, ion conduction, and chromatin biology.

C-D modes of deuterated side chain of leucine as structural reporters via dual-frequency two-dimensional infrared spectroscopy.

Residue-specific structural kinetics of proteins through the union of isotope labeling, mid-IR pulse shaping, and coherent 2D IR spectroscopy.

Computational design and biophysical characterization of aggregation-resistant point mutations for γD crystallin illustrate a balance of conformational stability and intrinsic aggregation propensity.

Proteomic analysis of human age-related nuclear cataracts and normal lens nuclei.

Intersheet rearrangement of polypeptides during nucleation of {beta}-sheet aggregates.

Ageing and vision: structure, stability and function of lens crystallins.

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221826493

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22328156

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3295317

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