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

Chem Phys Lipids. 2004 Nov;132(1):133-44. doi: 10.1016/j.chemphyslip.2004.09.018.

Abstract

Dipolar waves are distinct hallmarks of both the secondary and tertiary structures of alpha-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 alpha-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.

Publication types

  • Comparative Study
  • Evaluation Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Algorithms*
  • Binding Sites
  • Calcium-Binding Proteins / analysis
  • Calcium-Binding Proteins / chemistry*
  • Computer Simulation
  • Magnetic Resonance Spectroscopy / methods*
  • Membrane Proteins / analysis
  • Membrane Proteins / chemistry*
  • Models, Chemical*
  • Models, Molecular*
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Secondary

Substances

  • Calcium-Binding Proteins
  • Membrane Proteins
  • phospholamban