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, Stanley J. Opella

Research output: Contribution to journalArticlepeer-review

89 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)8928-8935
Number of pages8
JournalJournal of the American Chemical Society
Volume125
Issue number29
DOIs
StatePublished - Jul 23 2003

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