Year: 2025
Type: article
Abstract: A topological analysis was performed by taking ESEEM measurements of site-specifically labeled E protein from SARS-CoV-2. The intensity of deuterium modulation arising from either deuterated solvent or deuterated lipid acyl chains revealed exposure to solvent or the bilayer hydrophobic region. Spin-labeled lipids and soluble spin labels were used as points of comparison. The data indicate that spin labels placed along the transmembrane helix of the E protein showed close contact with lipid acyl chains, but also substantial contact with solvent, while those placed on the C-terminal domain showed substantial but lower exposure to lipid acyl chains, with comparable solvent exposure. The results support the view that the C-terminal domain is in contact with the bilayer surface.
Source: Biophysica
Authors: Andrew K. Morris, Robert M. McCarrick, Gary A. Lorigan
Institution: Miami University
Language: English
Subfield: Biophysics
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $1,207
OpenAlex ID: W4416721780