NDLI: Terahertz Spectroscopy of Bacteriorhodopsin and Rhodopsin: Similarities and Differences

Content Provider	PubMed Central
Author	Balu, R. Zhang, H. Zukowski, E. Chen, J. Y. Markelz, A. G. Gregurick, S. K.
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.
Related Links	http://dx.doi.org/10.1529/biophysj.107.105163
Ending Page	3226
Page Count	10
Starting Page	3217
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	8
Volume Number	94
Language	English
Publisher	The Biophysical Society
Publisher Date	2008-04-01
Access Restriction	Open
Rights Holder	The Biophysical Society
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

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Terahertz Spectroscopy of Bacteriorhodopsin and Rhodopsin: Similarities and Differences