Modulating Alignment of Membrane Proteins in Liquid-crystalline and Oriented Gel Media by Changing the Size and Charge of Phospholipid Bicelles

Overview

Journal J Biomol NMR

Publisher Springer

Specialties Molecular Biology
Nuclear Medicine

Date 2013 Mar 20

PMID 23508769

Citations 6

Authors

Justin L Lorieau

Alexander S Maltsev

John M Louis

Ad Bax

Affiliations

Soon will be listed here.

Abstract

We demonstrate that alignment of a structured peptide or small protein solubilized in mixed phospholipid:detergent micelles or bicelles, when embedded in a compressed gel or liquid crystalline medium, can be altered by either changing the phospholipid aggregate shape, charge, or both together. For the hemagglutinin fusion peptide solubilized in bicelles, we show that bicelle shape and charge do not change its helical hairpin structure but impact its alignment relative to the alignment medium, both in charged compressed acrylamide gel and in liquid crystalline d(GpG). The method can be used to generate sets of residual dipolar couplings that correspond to orthogonal alignment tensors, and holds promise for high-resolution structural refinement and dynamic mapping of membrane proteins.

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