Site-Directed Spin Labeling EPR Spectroscopy Of The Cytoplasmic Tail Of Influenza A M2
Document Type
Poster Session
Publication Date
2-15-2017
Published In
Biophysical Journal
Abstract
The M2 protein is a 97 residue homotetrameric, multifunctional ion channel that plays critical roles during the influenza infection cycle. While a variety of high-resolution biophysical techniques have been used to characterize the transmembrane domain (residues 22-46) and the juxtamembrane C-terminal region (46-62), less is known about the conformation and dynamics of the remaining residues of the C-terminal cytoplasmic tail. Here, we use site-directed spin labeling electron paramagnetic spectroscopy (SDSL-EPR) experiments to probe the secondary structure and membrane topology of cytoplasmic tail residues 60-80 when the protein is reconstituted into lipid bilayers. Cholesterol is essential for the role the C-terminal domain of the M2 protein plays in viral budding. SDSL-EPR data is collected in both in the presence and absence of cholesterol.
Recommended Citation
Alice L. Herneisen , '17; Grace Kim , '17; and Kathleen P. Howard.
(2017).
"Site-Directed Spin Labeling EPR Spectroscopy Of The Cytoplasmic Tail Of Influenza A M2".
Biophysical Journal.
Volume 112,
Issue 3, Supplement 1.
500a-500a.
DOI: 10.1016/j.bpj.2016.11.2705
https://works.swarthmore.edu/fac-chemistry/205