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Default Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.

Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.

Related Articles Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.

J Am Chem Soc. 2005 Sep 21;127(37):12965-74

Authors: Andronesi OC, Becker S, Seidel K, Heise H, Young HS, Baldus M

It is shown that molecular structure and dynamics of a uniformly labeled membrane protein can be studied under magic-angle-spinning conditions. For this purpose, dipolar recoupling experiments are combined with novel through-bond correlation schemes that probe mobile protein segments. These NMR schemes are demonstrated on a uniformly [13C,15N] variant of the 52-residue polypeptide phospholamban. When reconstituted in lipid bilayers, the NMR data are consistent with an alpha-helical trans-membrane segment and a cytoplasmic domain that exhibits a high degree of structural disorder.

PMID: 16159291 [PubMed - indexed for MEDLINE]



Source: PubMed
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