You have requested a machine translation of selected content from our databases. This functionality is provided solely for your convenience and is in no way intended to replace human translation. Neither SPIE nor the owners and publishers of the content make, and they explicitly disclaim, any express or implied representations or warranties of any kind, including, without limitation, representations and warranties as to the functionality of the translation feature or the accuracy or completeness of the translations.
Translations are not retained in our system. Your use of this feature and the translations is subject to all use restrictions contained in the Terms and Conditions of Use of the SPIE website.
14 March 2013Low-frequency dynamics of proteins and aqueous solutions studied by terahertz time-domain spectroscopy
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.