Terahertz spectroscopy of bacteriorhodopsin and rhodopsin: similarities and differences

Biophysical Journal
Radhakrishnan BaluSusan K Gregurick

Abstract

We studied the low-frequency terahertz spectroscopy of two photoactive protein systems, rhodopsin and bacteriorhodopsin, as a means to characterize collective low-frequency motions in helical transmembrane proteins. From this work, we found that the nature of the vibrational motions activated by terahertz radiation is surprisingly similar between these two structurally similar proteins. Specifically, at the lowest frequencies probed, the cytoplasmic loop regions of the proteins are highly active; and at the higher terahertz frequencies studied, the extracellular loop regions of the protein systems become vibrationally activated. In the case of bacteriorhodopsin, the calculated terahertz spectra are compared with the experimental terahertz signature. This work illustrates the importance of terahertz spectroscopy to identify vibrational degrees of freedom which correlate to known conformational changes in these proteins.

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Citations

Feb 4, 2009·Journal of Molecular Modeling·Saravana Prakash Thirumuruganandham, Herbert M Urbassek
Dec 20, 2008·Journal of Molecular Graphics & Modelling·Hailiang ZhangSusan K Gregurick
Nov 17, 2016·Scientific Reports·Kristina N WoodsJudith Klein-Seetharaman
Dec 7, 2011·Chemical Society Reviews·Alexander I McIntoshRobert S Donnan
May 8, 2018·Journal of Biological Physics·Z V GagkaevaB P Gorshunov
Aug 7, 2020·The Analyst·Zhongjie ZhuHongwei Zhao
Oct 8, 2020·Electromagnetic Biology and Medicine·Vasiliy N Kadantsev, Alexey Goltsov
Oct 25, 2014·The Journal of Physical Chemistry. B·Jun-Ho Choi, Minhaeng Cho
Oct 1, 2021·The Journal of Physical Chemistry Letters·Sreetama Pal, Amitabha Chattopadhyay

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