Conformational changes of photoactive yellow protein monitored by terahertz spectroscopy

被引:59
作者
Castro-Camus, E. [1 ]
Johnston, M. B. [1 ]
机构
[1] Univ Oxford, Dept Phys, Clarendon Lab, Oxford OX1 3PU, England
基金
英国工程与自然科学研究理事会;
关键词
D O I
10.1016/j.cplett.2008.02.084
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Observing the structural dynamics of proteins under conditions as close as possible to those in a living organism is essential for understanding the biological functions of proteins accurately. Here we demonstrate that terahertz spectroscopy is a convenient probe of conformational changes in proteins suspended in physiological buffer solution. We have observed that the partial unfolding of photoactive yellow protein leads to a clear increase in absorption at terahertz frequencies. Using normal mode and molecular dynamics simulations we show that this increase in absorption is related to an increase in the density of delocalised vibrational modes in the more flexible partially unfolded state. (c) 2008 Elsevier B. V. All rights reserved.
引用
收藏
页码:289 / 292
页数:4
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