What NMR can tell us about where lung surfactant proteins live

Biochem Soc Trans. 1997 Aug;25(3):1103-7. doi: 10.1042/bst0251103.

Abstract

2H-NMR is beginning to provide some insights into the way in which the hydrophobic surfactant proteins SP-B and SP-C interact with phospholipid bilayers in multilamellar structures. Both proteins have a significant effect on slow bilayer motions. In many ways, the effect of SP-C on the surrounding bilayer is similar to that of other transmembrane proteins. Ca2+ appears to modify the way in which SP-C perturbs the bilayers containing DPPG. The effect of SP-B on bilayers differs, in subtle ways, from that expected for a transmembrane protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1,2-Dipalmitoylphosphatidylcholine
  • Animals
  • Deuterium
  • Humans
  • Lipid Bilayers*
  • Lung / chemistry
  • Lung / physiology*
  • Nuclear Magnetic Resonance, Biomolecular / methods
  • Phosphatidylglycerols
  • Proteolipids / chemistry*
  • Pulmonary Surfactants / chemistry*

Substances

  • Lipid Bilayers
  • Phosphatidylglycerols
  • Proteolipids
  • Pulmonary Surfactants
  • 1,2-Dipalmitoylphosphatidylcholine
  • Deuterium
  • 1,2-dipalmitoylphosphatidylglycerol