Terahertz measurements of protein relaxational dynamics

被引：35

作者：

Knab, Joseph R. ^{[1
]}

Chen, Jing-Yin ^{[1
]}

He, Yunfen ^{[1
]}

Markelz, Andrea G. ^{[1
]}

机构：

[1] SUNY Buffalo, Dept Phys, Buffalo, NY 14260 USA

来源：

PROCEEDINGS OF THE IEEE | 2007年 / 95卷 / 08期

关键词：

biomolecules; dynamics; picosecond; terahertz;

D O I：

10.1109/JPROC.2007.898906

中图分类号：

TM [电工技术]; TN [电子技术、通信技术];

学科分类号：

0808 ; 0809 ;

摘要：

Collective structural vibrational modes of proteins lay in the terahertz frequency range. We discuss several measurements exploring picosecond dynamics in hen egg white lysozyme suggesting that terahertz time domain spectroscopy can provide unique insight to critical protein dynamics. We find a rapid increase in terahertz absorbance and index at both a critical hydration point and separately a critical temperature. Specifically, we discuss the hydration and temperature transitions and suggest that these are possibly linked. We discuss the possibility that the terahertz response is mainly determined by relaxational response of side chains within the protein and the energy barriers for these motions are hydration dependent. Finally we show that simple normal mode calculations do not reproduce the strong hydration dependence, further suggesting that resonant vibrational response is not sufficient to describe the terahertz dielectric response.

引用

页码：1605 / 1610

页数：6

共 21 条

[1] NORMAL-MODES FOR SPECIFIC MOTIONS OF MACROMOLECULES - APPLICATION TO THE HINGE-BENDING MODE OF LYSOZYME [J].