Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban

Alessandro Mascioni, Christine B Karim, Jamillah Zamoon, David D Thomas, Gianluigi Veglia

Research output: Contribution to journalArticlepeer-review

63 Scopus citations

Abstract

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°, ruling out the possibility of a continuous α-helical structure for this protein.

Original languageEnglish (US)
Pages (from-to)9392-9393
Number of pages2
JournalJournal of the American Chemical Society
Volume124
Issue number32
DOIs
StatePublished - Aug 14 2002

Fingerprint Dive into the research topics of 'Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban'. Together they form a unique fingerprint.

Cite this