Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban.
Solid-state NMR spectroscopy, in conjunction with rigid body molecular dynamics calculations, shows that monomeric phospholamban in lipid bilayers has two distinct helical domains, with an interhelical angle within 60-100 degrees, ruling out the possibility of a continuous alpha-helical structure for this protein.
Mascioni
Alessandro
A
Department of Chemistry, University of Minnesota, Minneapolis 55455, USA.
Karim
Christine
C
Zamoon
Jamillah
J
Thomas
David D
DD
Veglia
Gianluigi
G
D002135:Calcium-Binding Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D000099211:Phospholamban
D002135:Calcium-Binding Proteins; D000099211:Phospholamban