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 proteinsAssessment of amide I spectroscopic maps for a gas-phase peptide using IR-UV double-resonance spectroscopy and density functional theory calculationsSpatially Resolved Two-Dimensional Infrared Spectroscopy via Wide-Field MicroscopyMid-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 spectroscopyThermally 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 photodamageStudy 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 structureAn 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 inhibitorEvidence 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.
P2860
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P2860
Two-dimensional IR spectroscopy and segmental 13C labeling reveals the domain structure of human γD-crystallin amyloid fibrils.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.
@ast
Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.
@en
type
label
Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.
@ast
Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.
@en
prefLabel
Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.
@ast
Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.
@en
P2093
P2860
P356
P1476
Two-dimensional IR spectroscop ...... γD-crystallin amyloid fibrils.
@en
P2093
Ann Marie Woys
Lauren E Buchanan
Martin T Zanni
Sean D Moran
Sean M Decatur
P2860
P304
P356
10.1073/PNAS.1117704109
P407
P577
2012-02-10T00:00:00Z