The DOI matches its Crossref record.
Structure of the Amide I Band of Peptides Measured by Femtosecond Nonlinear-Infrared Spectroscopy
Abstract
Femtosecond infrared (IR) pump probe and dynamic hole burning experiments were used to examine the ultrafast response of the modes in the 1600−1700 cm -1 region (the so-called amide I modes) of N -methylacetamide (NMA) and three small globular peptides, apamin, scyllatoxin, and bovine pancreatic trypsin inhibitor (BPTI). A value of 16 cm -1 was found for the anharmonicity of the amide I vibration. Vibrational relaxation of the amide I modes of all investigated peptides occurs in ca. 1.2 ps. An even faster value of 450 fs is obtained for NMA, a model for the peptide unit. The vibrational relaxation is dominated by intramolecular energy redistribution (IVR) and reflects an intrinsic property of the peptide group in any environment. Dynamic hole burning experiments with a narrow band pump pulse which selectively excites only a subset of the amide I eigenstates reveal that energy migration between different amide I states is slow compared with vibrational relaxation. Two-dimensional pump−probe (2D-IR) spectra that display the spectral response of the amide I band as a function of the frequency of the narrow band pump pulse show that the amide I states are nevertheless delocalized along the peptide backbone. A simple excitonic coupling model describes the nonlinear pump−probe spectrum, and it reproduces the experimental 2D-IR spectra. It is estimated that the accessible peptide excitons are delocalized over a length of ca. 8 Å.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Infrared spectroscopy of proteins
Barth, A. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.06.004 · Cited by 5,129
“…effects: (i) Exciton transfer : if energy is absorbed by an oscillator it does not remain there but is rather transferred to a nearby oscillator with a typical time constant of 0.5 ps for an α - helix [178] — as a consequence the excited state is delocalised, typically over a length of 8 Å [178].”
BackgroundInfluentialWhat vibrations tell about proteins
Barth, A., & Zscherp, C. (2002) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583502003815 · Cited by 2,088
Water Dynamics in the Hydration Shells of Biomolecules
Laage, D., Elsaesser, T., & Hynes, J. T. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00765 · Cited by 913
Multidimensional Femtosecond Correlation Spectroscopies of Electronic and Vibrational Excitations
Mukamel, S. (2000) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.51.1.691 · Cited by 894
Tanimura, Y. (2006) · Journal of the Physical Society of Japan · doi:10.1143/jpsj.75.082001 · Cited by 891
Coherent Two-Dimensional Optical Spectroscopy
Cho, M. (2008) · Chemical Reviews · doi:10.1021/cr078377b · Cited by 835
Asplund, M. C., Zanni, M. T., & Hochstrasser, R. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.140227997 · Cited by 512
Self-citationUltrafast Spectroscopy: State of the Art and Open Challenges
Maiuri, M., Garavelli, M., & Cerullo, G. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b10533 · Cited by 460
Vibrational Spectroscopic Map, Vibrational Spectroscopy, and Intermolecular Interaction
Baiz, C. R., Błasiak, B., Bredenbeck, J., Cho, M., Choi, J.-H., Corcelli, S. A., Dijkstra, A. G., Feng, C.-J., Garrett-Roe, S., Ge, N.-H., et al. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00813 · Cited by 412
Real-Time Observation of Organic Cation Reorientation in Methylammonium Lead Iodide Perovskites
Bakulin, A. A., Selig, O., Bakker, H. J., Rezus, Y. L. A., Müller, C., Glaser, T., Lovrincic, R., Sun, Z., Chen, Z., Walsh, A., et al. (2015) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.5b01555 · Cited by 372
Infrared Difference Spectroscopy of Proteins: From Bands to Bonds
Lorenz-Fonfria, V. A. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00449 · Cited by 325
Shim, S.-H., Strasfeld, D. B., Ling, Y. L., & Zanni, M. T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700804104 · Cited by 314
Stimulated Electronic X-Ray Raman Scattering
Weninger, C., Purvis, M., Ryan, D., London, R. A., Bozek, J. D., Bostedt, C., Graf, A., Brown, G., Rocca, J. J., & Rohringer, N. (2013) · Physical Review Letters · doi:10.1103/physrevlett.111.233902 · Cited by 148
Ishizaki, A., & Tanimura, Y. (2006) · The Journal of Chemical Physics · doi:10.1063/1.2244558 · Cited by 115
Quantum coherence in ion channels: resonances, transport and verification
Vaziri, A., & Plenio, M. B. (2010) · New Journal of Physics · doi:10.1088/1367-2630/12/8/085001 · Cited by 88
Cao, W., Warrick, E. R., Fidler, A., Neumark, D. M., & Leone, S. R. (2016) · Physical Review A · doi:10.1103/physreva.94.053846 · Cited by 71
Zhuang, W., Cui, R. Z., Silva, D.-A., & Huang, X. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp109592b · Cited by 70
Probing the heterogeneous structure of eumelanin using ultrafast vibrational fingerprinting
Grieco, C., Kohl, F. R., Hanes, A. T., & Kohler, B. (2020) · Nature Communications · doi:10.1038/s41467-020-18393-w · Cited by 62
Time-Resolved Studies of Water Dynamics and Proton Transfer at the Alumina−Air Interface
Le Caër, S., Palmer, D. J., Lima, M., Renault, J. P., Vigneron, G., Righini, R., & Pommeret, S. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0691730 · Cited by 25
Metadata
- Authors
- Hamm, P., Lim, M., & Hochstrasser, R. M.
- Venue
- The Journal of Physical Chemistry B
- Publisher
- American Chemical Society (ACS)
- Published
- 1998-06-11
- Volume
- 102
- Issue
- 31
- Pages
- 6123-6138
- ISSN
- 1520-5207 (ISSN-L)
- 1520-6106
- OpenAlex
- W2042998938
- Cited by
- 1,096
- References
- 0
- FWCI
- 16.44
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
