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THz time domain spectroscopy of biomolecular conformational modes
Open accessAbstract
We discuss the use of terahertz time domain spectroscopy for studies of conformational flexibility and conformational change in biomolecules. Protein structural dynamics are vital to biological function with protein flexibility affecting enzymatic reaction rates and sensory transduction cycling times. Conformational mode dynamics occur on the picosecond timescale and with the collective vibrational modes associated with these large scale structural motions in the 1-100 cm(-1) range. We have performed THz time domain spectroscopy (TTDS) of several biomolecular systems to explore the sensitivity of TTDS to distinguish different molecular species, different mutations within a single species and different conformations of a given biomolecule. We compare the measured absorbances to normal mode calculations and find that the TTDS absorbance reflects the density of normal modes determined by molecular mechanics calculations, and is sensitive to both conformation and mutation. These early studies demonstrate some of the advantages and limitations of using TTDS for the study of biomolecules.
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Bahri, S. W. S., Addis, S., Munajat, N. F., Kasim, N., & Zakaria, H. A. (2024) · Journal of Advanced Research in Applied Sciences and Engineering Technology · doi:10.37934/araset.43.1.160170
Wang, Y., Hu, Y., Meng, J., Peng, X., & Zhao, Q. C. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.28.591535
Modulation of terahertz absorption by a single mutation of rhodopsin mimics
Wang, Y., Hu, Y., Meng, J., Peng, X., & Zhao, Q. B. (2025) · Physical Chemistry Chemical Physics · doi:10.1039/d4cp04411h
Frequency range converter modules 50–178.4 GHz for vector network analyzers
Muravev, V. M., Zarezin, A. M., Titenko, A. A., Bobova, V. D., Sinogin, M. V., Кукушкин, И. В., & Заостровных, С. (2025) · Izmeritel`naya Tekhnika · doi:10.32446/0368-1025it.2025-4-55-63
Frequency range converter modules 50–178.4 GHz for vector network analyzers
Muravev, V. M., Zarezin, A. M., Titenko, A. A., Bobova, V. D., Sinogin, M. V., Кукушкин, И. В., & Заостровных, С. (2025) · Measurement Techniques · doi:10.1007/s11018-025-02465-8
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Liu, K., Zhang, J., Zhang, G., Sun, L., & Liu, W. (2025) · Chinese Journal of Chemical Physics · doi:10.1063/1674-0068/cjcp2507106
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Zhao, J., Chen, S., Wang, X., Qian, Z., & Fan, S. (2025) · Applied Physics Letters · doi:10.1063/5.0308528
Imagerie et spectroscopie térahertz : application aux problématiques de défense et de sécurité
Sleiman, J. B. (2016) · theses.fr (ABES) · doi:10.70675/f5e86d4ez519dz42e0z9094z78d23f801e67
Metadata
- Authors
- Markelz, A., Whitmire, S., Hillebrecht, J., & Birge, R.
- Affiliations
- University at Buffalo, State University of New York (US)
- University of Connecticut (US)
- ORCID
- Markelz, Andrea
- Venue
- Physics in Medicine and Biology
- Publisher
- IOP Publishing
- Published
- 2002-10-16
- Volume
- 47
- Issue
- 21
- Pages
- 3797-3805
- ISSN
- 0031-9155 (ISSN-L)
- OpenAlex
- W2116459310
- Cited by
- 309
- References
- 24
- Citations by year
- 2026: 4 · 2025: 12 · 2024: 9 · 2023: 7 · 2022: 16 · 2021: 14 · 2020: 14 · 2019: 19 · 2018: 16 · 2017: 12 · 2016: 19 · 2015: 14 · 2014: 12 · 2013: 19 · 2012: 15
- FWCI
- 8.39
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Physics in Medicine and Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM034548)
- Army Research Office
- Topics
- Physical Sciences › Engineering › Electrical and Electronic Engineering › Terahertz technology and applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Spectroscopy Techniques in Biomedical and Chemical Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- terahertz time-domain spectroscopy, protein structural dynamics, conformational change, normal mode analysis, molecular mechanics, protein mutations, vibrational modes
- MeSH terms
- Animals, Bacteriorhodopsins, Crystallography, Microwaves, Muramidase, Myocardium, Myoglobin, Photic Stimulation, Protein Conformation, Proteins, Sensitivity and Specificity, Species Specificity, Spectrum Analysis, Temperature, Halobacterium salinarum, Macromolecular Substances, Optics and Photonics
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