Key result
ATR-FTIR spectroscopy and isotope labeling reveal the phospholamban transmembrane domain is predominantly alpha-helical and lipid-embedded.
Population
Hydrophobic C-terminal 28 amino acid fragment of phospholamban reconstituted into…
Design
Preclinical
Authors
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Refines phospholamban membrane topology models; extends biophysical data but leaves open clinical translation to heart failure.
ATR-FTIR spectroscopy and isotope labeling confirm that the transmembrane domain of phospholamban forms an alpha-helical structure embedded in the lipid bilayer.
Ludlam et al. (1996) studied this question. Site-directed isotope labeling and ATR-FTIR spectroscopy was evaluated on Local secondary structure and orientation of the transmembrane domain of phospholamban. ATR-FTIR spectroscopy and site-directed isotope labeling demonstrated that the transmembrane domain of phospholamban is predominantly alpha-helical and embedded in the lipid bilayer.
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