14 March 2013 Low-frequency dynamics of proteins and aqueous solutions studied by terahertz time-domain spectroscopy
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Abstract
We studied low-frequency spectra of hydration water molecules around the hydrophobic probe in an aqueous solution by using tetraalkylammonium cation as a probe and terahertz time-domain spectroscopic technique. The phenomenon, called dynamical transition, has been known to be universally observed among proteins and polypeptides. In this work we investigated temperature and hydration dependence of low-frequency dynamics to clarify relationships between the dynamical transition and protein structures, and its functional states. We also mention general behaviors of the lowfrequency spectra of globular proteins.
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Naoki Yamamoto, Naoki Yamamoto, Akané Ishihara, Akané Ishihara, Azusa Kaneko, Azusa Kaneko, Haruka Iguchi, Haruka Iguchi, Ohki Kambara, Ohki Kambara, Atsuo Tamura, Atsuo Tamura, Keisuke Tominaga, Keisuke Tominaga, } "Low-frequency dynamics of proteins and aqueous solutions studied by terahertz time-domain spectroscopy", Proc. SPIE 8623, Ultrafast Phenomena and Nanophotonics XVII, 862306 (14 March 2013); doi: 10.1117/12.2007253; https://doi.org/10.1117/12.2007253
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