Determination of helical membrane protein topology using residual dipolar couplings and exhaustive search algorithm: Application to phospholamban

Alessandro Mascioni, Becky L. Eggimann, Gianluigi Veglia

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Dipolar waves are distinct hallmarks of both the secondary and tertiary structures of α-helical proteins that are immobilized in membrane bilayers or embedded in anisotropic media. We present a simple, semi-empirical approach that exploits the modulation of the amplitude and average of dipolar waves to determine the topology of α-helical proteins. Moreover, we describe the application of this method for the structural determination of a detergent solubilized membrane protein, phospholamban (PLB) that is involved in calcium regulation of cardiac muscle. When combined with high-resolution solid-state NMR data, this method can serve as a fast route for determining the topology of helical membrane proteins solubilized in detergent micelles.

Original languageEnglish (US)
Pages (from-to)133-144
Number of pages12
JournalChemistry and Physics of Lipids
Volume132
Issue number1
DOIs
StatePublished - Oct 1 2004

Keywords

  • Ca-ATPase
  • DPC micelles
  • Dipolar waves
  • Exhaustive search
  • Helical wheels
  • Membrane proteins
  • NMR
  • Phospholamban
  • Polyacrylamide gel
  • Residual dipolar couplings
  • SERCA
  • α-Helix

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