| Literature DB >> 16159291 |
Ovidiu C Andronesi1, Stefan Becker, Karsten Seidel, Henrike Heise, Howard S Young, Marc Baldus.
Abstract
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.Entities:
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Year: 2005 PMID： 16159291 DOI： 10.1021/ja0530164
Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419