ArticleThe journal of physical chemistry. B2008
Two-dimensional infrared spectroscopy as a probe of the solvent electrostatic field for a twelve residue peptide.
Article in The journal of physical chemistry. B, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Vibrational Spectroscopic Map, Vibrational Spectroscopy, and Intermolecular Interaction.Chemical reviews · 2020Review
- Solvent-Independent Anharmonicity for Carbonyl Oscillators.The journal of physical chemistry. B · 2017Article
- Two-Dimensional Infrared (2DIR) Spectroscopy of the Peptide Beta3s Folding.The journal of physical chemistry letters · 2013Article
- 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.Journal of the American Chemical Society · 2012Article
- Development and validation of transferable amide I vibrational frequency maps for peptides.The journal of physical chemistry. B · 2011Article
- Discriminating early stage A{beta}42 monomer structures using chirality-induced 2DIR spectroscopy in a simulation study.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- 2D IR provides evidence for mobile water molecules in beta-amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Sensitivity of 2D IR spectra to peptide helicity: a concerted experimental and simulation study of an octapeptide.The journal of physical chemistry. B · 2009Article
- 2D-IR experiments and simulations of the coupling between amide-I and ionizable side chains in proteins: application to the Villin headpiece.The journal of physical chemistry. B · 2009Article
- Folding mechanism of β-hairpin trpzip2: heterogeneity, transition state and folding pathways.International journal of molecular sciences · 2009Review
- Equilibrium exchange processes of the aqueous tryptophan dipeptide.The journal of physical chemistry. B · 2009Article
- Applications of 2D IR spectroscopy to peptides, proteins, and hydrogen-bond dynamics.The journal of physical chemistry. B · 2009Article
- Empirical amide I vibrational frequency map: application to 2D-IR line shapes for isotope-edited membrane peptide bundles.The journal of physical chemistry. B · 2009Review
- 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
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Authors and funding
4 authors.
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Abstract
The linear IR and two-dimensional (2D) IR spectra of the amide-I modes of the 12-residue beta-hairpin peptide tryptophan zipper-2 (SWTWENGKWTWK) and its two 13C isotopomers were simulated, with local mode frequencies evaluated by two solution-phase peptide amide-I frequency maps proposed recently: an electrostatic potential map and an electrostatic field map. Both maps predict a set of nondegenerate local amide-I mode transition energies for the hairpin. Spectral simulations using both maps predict the main spectral features of the linear IR and 2D IR experimental results of the (13)C-labeled and -unlabeled hairpin. The radial distribution functions obtained using trajectories from classical molecular dynamics simulations demonstrate different water distributions at different sites of the hairpin. Our results suggest that the observed difference of the (13)C-shifted band, including its peak position and frequency distributions for different isotopomers, in both linear IR and 2D IR spectra, is likely to be due to the difference in the local environment of the solvated peptide. Ab initio density functional theory calculations show a residue-independent (13)C shift of the amide-I mode, further supporting the result. The variations of these shifts are attributed to the residue level heterogeneity of the electrostatic environment of the peptide. Our results show that 2D IR of peptide with single (13)C isotopic labeling can be used to probe the electrostatic environment of the peptide local structure.
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