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J Am Chem Soc. 2009 Oct 14;131(40):14140-1. doi: 10.1021/ja905640d.

Phage-induced alignment of membrane proteins enables the measurement and structural analysis of residual dipolar couplings with dipolar waves and lambda-maps.

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1
Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093-0307, USA.

Abstract

At pH > 6 added filamentous bacteriophage fd is compatible with many of the detergents used to solubilize membrane proteins for solution NMR studies of membrane proteins and, therefore, serves as an alignment media. In combination with strained polyacrylamide gel alignment, Dipolar Waves can be used to directly assess the secondary structure and a lambda-map extracts the order tensors for de novo structure calculation of membrane proteins without distance restraints.

PMID:
19761238
PMCID:
PMC2771775
DOI:
10.1021/ja905640d
[Indexed for MEDLINE]
Free PMC Article
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