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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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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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