ArticleThe journal of physical chemistry letters2011
Utilizing Lifetimes to Suppress Random Coil Features in 2D IR Spectra of Peptides.
Article in The journal of physical chemistry letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed, 40 citations in OpenAlex.
- Characterization of dynamics of encapsulated small molecule Nile red in biodegradable polymer using 2D IR methods.The Journal of chemical physics · 2026Article
- Suppressing sidechain modes and improving structural resolution for 2D IR spectroscopy via vibrational lifetimes.The Journal of chemical physics · 2024Article
- Liquid-Liquid Phase Separation of the Intrinsically Disordered Domain of the Fused in Sarcoma Protein Results in Substantial Slowing of Hydration Dynamics.The journal of physical chemistry letters · 2023Article
- Modulation of IL-17 backbone dynamics reduces receptor affinity and reveals a new inhibitory mechanism.Chemical science · 2023Article
- Direct observation of protein structural transitions through entire amyloid aggregation processes in water using 2D-IR spectroscopy.Chemical science · 2022Article
- Cross-α/β polymorphism of PSMα3 fibrils.Proceedings of the National Academy of Sciences of the United States of America · 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
- Photon echoes and two dimensional spectra of the amide I band of proteins measured by femtosecond IR - Raman spectroscopy.Chemical science · 2020Article
- Unperturbed Detection of the Dynamic Structure in the Hydrophobic Core of Trp-Cage via Two-Dimensional Infrared Spectroscopy.The journal of physical chemistry letters · 2020Article
- Measuring proteins in HChemical science · 2019Article
- Ultrafast energy relaxation dynamics of amide I vibrations coupled with protein-bound water molecules.Nature communications · 2019Article
- Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Chemical reviews · 2017Review
- Computing infrared spectra of proteins using the exciton model.Journal of computational chemistry · 2017Article
- Spatially Resolved Two-Dimensional Infrared Spectroscopy via Wide-Field Microscopy.ACS photonics · 2016Article
- Transition Dipoles from 1D and 2D Infrared Spectroscopy Help Reveal the Secondary Structures of Proteins: Application to Amyloids.The journal of physical chemistry. B · 2015Article
- Theoretical Sum Frequency Generation Spectroscopy of Peptides.The journal of physical chemistry. B · 2015Article
- Heterogeneous preferential solvation of water and trifluoroethanol in homologous lysozymes.The journal of physical chemistry. B · 2014Article
- How to Get Insight into Amyloid Structure and Formation from Infrared Spectroscopy.The journal of physical chemistry letters · 2014Review
- Two-dimensional sum-frequency generation reveals structure and dynamics of a surface-bound peptide.Journal of the American Chemical Society · 2014Article
- Intrinsic structural heterogeneity and long-term maturation of amyloid β peptide fibrils.ACS chemical neuroscience · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We report that the waiting time delay in 2D IR pulse sequences can be used to suppress signals from structurally disordered regions of amyloid fibrils. At a waiting time delay of 1.0 ps, the random coil vibrational modes of amylin fibrils are no longer detectable, leaving only the sharp excitonic vibrational features of the fibril β-sheets. Isotope labeling with (13)C(18)O reveals that structurally disordered residues decay faster than residues protected from solvent. Since structural disorder is usually accompanied by hydration, we conclude that the shorter lifetimes of random-coil residues is due to solvent exposure. These results indicate that 2D IR pulse sequences can utilize the waiting time to better resolve solvent-protected regions of peptides and that local mode lifetimes should be included in simulations of 2D IR spectra.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.