Incorporation of transmembrane peptides from the vacuolar H(+)-ATPase in phospholipid membranes: spin-label electron paramagnetic resonance and polarized infrared spectroscopy

Zoltán Kóta, Tibor Páli, Neil Dixon, Terry P. Kee, Michael A. Harrison, John B.C. Findlay, Malcolm E. Finbow, Derek Marsh

Research output: Contribution to journalArticle


Peptides were designed that are based on candidate transmembrane sequences of the Vo-sector from the vacuolar H+-ATPase of Saccharomyces cerevisiae. Spin-label EPR studies of lipid–protein interactions were used to characterize the state of oligomerization, and polarized IR spectroscopy was used to determine the secondary structure and orientation, of these peptides in lipid bilayer membranes. Peptides corresponding to the second and fourth transmembrane domains (TM2 and TM4) of proteolipid subunit c (Vma3p) and of the putative seventh transmembrane domain (TM7) of subunit a (Vph1p) are wholly, or predominantly, a-helical in membranes of dioleoyl phosphatidylcholine.

Original languageEnglish
Pages (from-to)3937-3949
Number of pages13
Issue number12
Publication statusPublished - 1 Feb 2008



  • biochemistry
  • transmembrane peptides
  • phospholipid membranes
  • ATPase

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