The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Vibrational Stark Effects Calibrate the Sensitivity of Vibrational Probes for Electric Fields in Proteins
Abstract
Infrared spectroscopy is widely used to probe local environments and dynamics in proteins. The introduction of a unique vibration at a specific site of a protein or more complex assembly offers many advantages over observing the spectra of an unmodified protein. We have previously shown that infrared frequency shifts in proteins can arise from differences in the local electric field at the probe vibration. Thus, vibrational frequencies can be used to map electric fields in proteins at many sites or to measure the change in electric field due to a perturbation. The Stark tuning rate gives the sensitivity of a vibrational frequency to an electric field, and for it to be useful, the Stark tuning rate should be as large as possible. Vibrational Stark effect spectroscopy provides a direct measurement of the Stark tuning rate and allows a quantitative interpretation of frequency shifts. We present vibrational Stark spectra of several bond types, extending our work on nitriles and carbonyls and characterizing four additional bond types (carbon-fluorine, carbon-deuterium, azide, and nitro bonds) that are potential probes for electric fields in proteins. The measured Stark tuning rates, peak positions, and extinction coefficients provide the primary information needed to design amino acid analogues or labels to act as probes of local environments in proteins.
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Cites
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The infrared absorption of amino acid side chains
Barth, A. (2000) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(00)00021-3 · Cited by 1,355
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STARK SPECTROSCOPY: Applications in Chemistry, Biology, and Materials Science
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Self-citationStructure and dynamics of membrane proteins as studied by infrared spectroscopy
Arrondo, J. L. R., & Goñi, F. M. (1999) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(99)00007-3 · Cited by 426
Large Molecular Third-Order Optical Nonlinearities in Polarized Carotenoids
Marder, S. R., Torruellas, W. E., Blanchard-Desce, M., Ricci, V., Stegeman, G. I., Gilmour, S., Brédas, J., Li, J., Bublitz, G. U., & Boxer, S. G. (1997) · Science · doi:10.1126/science.276.5316.1233 · Cited by 402
Self-citationUsing Nitrile-Derivatized Amino Acids as Infrared Probes of Local Environment
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Vibrational Stark Spectroscopy in Proteins: A Probe and Calibration for Electrostatic Fields
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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
A chemical toolkit for proteins — an expanded genetic code
Xie, J., & Schultz, P. G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2005 · Cited by 408
Metadata
- Authors
- Suydam, I. T., & Boxer, S. G.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-09-26
- Volume
- 42
- Issue
- 41
- Pages
- 12050-12055
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2136751388
- Cited by
- 262
- References
- 20
- FWCI
- 3.41
- Type
- journal article
- Language
- en
- Open access
- closed
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