ArticleBiophysical journal2008
Terahertz spectroscopy of bacteriorhodopsin and rhodopsin: similarities and differences.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 72 citations in OpenAlex.
- Epithelial Sodium Channel Inhibition by Amiloride Addressed with THz Spectroscopy and Molecular Modeling.Molecules (Basel, Switzerland) · 2022Article
- Broadband terahertz recognizing conformational characteristics of a significant neurotransmitter γ-aminobutyric acid.RSC advances · 2019Article
- Terahertz Spectroscopy and Imaging: A Cutting-Edge Method for Diagnosing Digestive Cancers.Materials (Basel, Switzerland) · 2019Review
- Terahertz-infrared spectroscopy of Shewanella oneidensis MR-1 extracellular matrix.Journal of biological physics · 2018Article
- Terahertz Frequency Spectroscopy to Determine Cold Shock Protein Stability upon Solvation and Evaporation - A Molecular Dynamics Study.IEEE transactions on terahertz science and technology · 2017Article
- Vibrational resonance, allostery, and activation in rhodopsin-like G protein-coupled receptors.Scientific reports · 2016Article
- Dielectric relaxation dynamics of water in model membranes probed by terahertz spectroscopy.Biophysical journal · 2009Article
- Rhodopsin: the functional significance of asn-linked glycosylation and other post-translational modifications.Ophthalmic genetics · 2009Review
- Low-frequency vibrational modes and infrared absorbance of red, blue and green opsin.Journal of molecular modeling · 2009Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.