Work

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

Year: 2003

Type: article

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 alpha-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.

Source: Journal of the American Chemical Society

DOI: 10.1021/ja034211q

Authors: Michael F. Mesleh, Sangwon Lee, Gianluigi Veglia, David S. Thiriot, Francesca M. Marassi, Stanley J. Opella

Institutions: University of Minnesota, Sanford Burnham Prebys Medical Discovery Institute, University of California San Diego

Language: English

Topic: Advanced NMR Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: National Cancer Institute, National Institute of General Medical Sciences, National Institute of Biomedical Imaging and Bioengineering, National Center for Research Resources