ArticleBiophysical journal2006
Two-dimensional infrared spectroscopy displays signatures of structural ordering in peptide aggregates.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Protein-Membrane Interactions Studied by Transmission and Total Internal Reflection FTIR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Frequency Changes in Terminal Alkynes Provide Strong, Sensitive, and Solvatochromic Raman Probes of Biochemical Environments.The journal of physical chemistry. B · 2023Article
- Structure Changes of a Membrane Polypeptide under an Applied Voltage Observed with Surface-Enhanced 2D IR Spectroscopy.The journal of physical chemistry letters · 2021Article
- Vibrational Approach to the Dynamics and Structure of Protein Amyloids.Molecules (Basel, Switzerland) · 2019Review
- How to Get Insight into Amyloid Structure and Formation from Infrared Spectroscopy.The journal of physical chemistry letters · 2014Review
- Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage.Biochemistry · 2013Article
- Spectroscopic studies of protein folding: linear and nonlinear methods.Protein science : a publication of the Protein Society · 2012Review
- Utilizing Lifetimes to Suppress Random Coil Features in 2D IR Spectra of Peptides.The journal of physical chemistry letters · 2011Article
- Strategies for extracting structural information from 2D IR spectroscopy of amyloid: application to islet amyloid polypeptide.The journal of physical chemistry. B · 2009Article
- Two-dimensional infrared spectra of isotopically diluted amyloid fibrils from Abeta40.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Two-dimensional spectroscopy at infrared and optical frequencies.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Amide vibrations are delocalized across the hydrophobic interface of a transmembrane helix dimer.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Local structure of beta-hairpin isotopomers by FTIR, 2D IR, and ab initio theory.The journal of physical chemistry. B · 2006Article
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Authors and funding
4 authors.
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Abstract
In the presence of lipid bilayers, the hexapeptide AcWL(5) forms membrane-bound aggregates dominated by beta-secondary structure and is thus a useful model for the onset of peptide aggregation in membrane environments. Two-dimensional infrared (2D IR) spectra in the amide I region for aggregates of AcWL(5) peptides with single isotopic labels provide new insight into the residue-level structural ordering of the aggregated peptides. Separation of spectral information along two axes provides clear indications of the band frequencies and relative intensities, which together are an indication of extended amide coupling networks across structural regions of a particular size. The lowered anharmonicities, relative to free peptide, and the narrow, homogeneous lineshapes of the 2D IR peaks indicate the delocalization of vibrational modes through an ordered structure whose flexibility varies with relative peptide concentration. Crosspeaks between delocalized transitions can be used to estimate the strength of the coupling interactions between neighboring residues. The sensitivity of 2D IR spectra to residue-level structural ordering shows that 2D IR spectroscopy is a powerful technique for probing structures formed during the onset of peptide aggregation.
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