ArticleProceedings of the National Academy of Sciences of the United States of America2008
Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed.
- Protein-Membrane Interactions Studied by Transmission and Total Internal Reflection FTIR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Heterotypic Interactions of Amyloid β and the Islet Amyloid Polypeptide Produce Mixed Aggregates with Non-Native Fibril Structure.The journal of physical chemistry letters · 2024Article
- Suppressing sidechain modes and improving structural resolution for 2D IR spectroscopy via vibrational lifetimes.The Journal of chemical physics · 2024Article
- Probing local changes to α-helical structures with 2D IR spectroscopy and isotope labeling.Biophysical journal · 2023Article
- Investigating the effects of N-terminal acetylation on KFE8 self-assembly with 2D IR spectroscopy.Biophysical journal · 2022Article
- A Different hIAPP Polymorph Is Observed in Human Serum Than in Aqueous Buffer: Demonstration of a New Method for Studying Amyloid Fibril Structure Using Infrared Spectroscopy.The journal of physical chemistry letters · 2020Article
- Monolayer Sensitivity Enables a 2D IR Spectroscopic Immuno-biosensor for Studying Protein Structures: Application to Amyloid Polymorphs.The journal of physical chemistry letters · 2019Article
- Glutamine Side ChainJournal of the American Chemical Society · 2019Article
- Amyloid found in human cataracts with two-dimensional infrared spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Vibrational Approach to the Dynamics and Structure of Protein Amyloids.Molecules (Basel, Switzerland) · 2019Review
- Structural Polymorphs Suggest Competing Pathways for the Formation of Amyloid Fibrils That Diverge from a Common Intermediate Species.Biochemistry · 2018Article
- Observation of Ultrafast Vibrational Energy Transfer in Fibrinogen and Fibrin Fibers.The journal of physical chemistry. B · 2018Article
- Two-Dimensional Spectroscopy Is Being Used to Address Core Scientific Questions in Biology and Materials Science.The journal of physical chemistry. B · 2018Review
- Site-specific detection of protein secondary structure using 2D IR dihedral indexing: a proposed assembly mechanism of oligomeric hIAPP.Chemical science · 2018Article
- Spectroscopic Signature for Stable β-Amyloid Fibrils versus β-Sheet-Rich Oligomers.The journal of physical chemistry. B · 2018Article
- Not All β-Sheets Are the Same: Amyloid Infrared Spectra, Transition Dipole Strengths, and Couplings Investigated by 2D IR Spectroscopy.The journal of physical chemistry. B · 2017Article
- Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Chemical reviews · 2017Review
- Kinetic Isotope Effect Provides Insight into the Vibrational Relaxation Mechanism of Aromatic Molecules: Application to Cyano-phenylalanine.The journal of physical chemistry letters · 2016Article
- Isotope-edited FTIR reveals distinct aggregation and structural behaviors of unmodified and pyroglutamylated amyloid β peptides.Physical chemistry chemical physics : PCCP · 2015Article
- A synchrotron-based hydroxyl radical footprinting analysis of amyloid fibrils and prefibrillar intermediates with residue-specific resolution.Biochemistry · 2014Article
4 more citing papers are in PubMed but not listed here.
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4 authors.
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Abstract
The 2D IR spectra of the amide-I vibrations of amyloid fibrils from Abeta40 were obtained. The matured fibrils formed from strands having isotopic substitution by (13)C (18)O at Gly-38, Gly-33, Gly-29, or Ala-21 show vibrational exciton spectra having reduced dimensionality. Indeed, linear chain excitons of amide units are seen, for which the interamide vibrational coupling is measured in fibrils grown from 50% and 5% mixtures of labeled and unlabeled strands. The data prove that the 1D excitons are formed from parallel in-register sheets. The coupling constants show that for each of the indicated residues the amide carbonyls in the chains are separated by 0.5 +/- 0.05 nm. The isotope replacement of Gly-25 does not reveal linear excitons, consistent with the region of the strand having a different structure distribution. The vibrational frequencies of the amide-I modes, freed from effects of amide vibrational excitation exchange by 5% dilution experiments, point to there being a component of an electric field along the fibril axis that increases through the sequence Gly-38, Gly-33, Gly-29. The field is dominated by side chains of neighboring residues.
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