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Proceedings Paper

Probe conformational dynamics of proteins in aqueous solutions by terahertz spectroscopy
Author(s): Nguyen Q. Vinh
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Paper Abstract

Proteins solvated in their biologically milieu are expected to exhibit strong absorption in the terahertz frequencies, that contain information on their global and sub-global collective vibrational modes (conformational dynamics) and global dynamic correlations among solvent water and proteins. The dynamics play an important role in enzymatic activities of proteins, but obtaining an accurate and quantitative pictures of these activities, however, is challenging due to the strong absorption of water. In response, we have developed the world’s highest precision, highest sensitivity terahertz-frequency domain spectrometer and a standard terahertz-time domain system to probe the collective dynamics of proteins in aqueous solutions. Operating over the frequency range from 5 GHz up to 3 THz, our spectrometers provide an unparalleled ability to probe directly such questions as the hydration level, the dynamics of water and hydrated proteins over the 100 fs to 1 ns timescale. Employing an effective medium approximation to describe the complex dielectric response of the solvated proteins in solution we find that proteins are surrounded by a loosely and tightly held layers of water molecules that behave as if they are an integral part of the protein. The number of water molecules in the protein hydration shells varies with proteins, which can tell us the average surface structure of proteins. These measurements shed light on the macromolecular motions of proteins in their biologically relevant environment.

Paper Details

Date Published: 26 October 2016
PDF: 8 pages
Proc. SPIE 9934, Terahertz Emitters, Receivers, and Applications VII, 99340R (26 October 2016); doi: 10.1117/12.2238597
Show Author Affiliations
Nguyen Q. Vinh, Virginia Polytechnic Institute and State Univ. (United States)

Published in SPIE Proceedings Vol. 9934:
Terahertz Emitters, Receivers, and Applications VII
Manijeh Razeghi; Alexei N. Baranov; John M. Zavada; Dimitris Pavlidis, Editor(s)

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