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Article

Dipolar Waves Map the Structure and Topology of Helices in Membrane Proteins

Michael F. Mesleh,^† Sangwon Lee,^† Gianluigi Veglia,^‡ David S. Thiriot,^† Francesca M. Marassi,^§ and Stanley J. Opella*^†

Contribution from the Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive La Jolla, California 92093, Department of Chemistry, University of Minnesota, Minneapolis, 207 Pleasant Street, Minnesota 53485, and The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, California 92037

J. Am. Chem. Soc., 2003, 125 (29), pp 8928–8935

DOI: 10.1021/ja034211q

Publication Date (Web): June 25, 2003

†

University of California, San Diego.

‡

University of Minnesota.

The Burnham Institute.

In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

sopella@ucsd.edu

Abstract

Dipolar waves describe the structure and topology of helices in membrane proteins. The fit of sinusoids with the 3.6 residues per turn period of ideal α-helices to experimental measurements of dipolar couplings as a function of residue number makes it possible to simultaneously identify the residues in the helices, detect kinks or curvature in the helices, and determine the absolute rotations and orientations of helices in completely aligned bilayer samples and relative rotations and orientations of helices in a common molecular frame in weakly aligned micelle samples. Since as much as 80% of the structured residues in a membrane protein are in helices, the analysis of dipolar waves provides a significant step toward structure determination of helical membrane proteins by NMR spectroscopy.

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