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

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

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

J Am Chem Soc. 2002 Aug 14;124(32):9392-3

Authors: Mascioni A, Karim C, Zamoon J, Thomas DD, Veglia G

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.

PMID: 12167032 [PubMed - indexed for MEDLINE]



Source: PubMed
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