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Methods Mol Biol. 2017;1500:203-215.

Designing DNA Nanotube Liquid Crystals as a Weak-Alignment Medium for NMR Structure Determination of Membrane Proteins.

Min J1,2,3, Shih WM2,4,5, Bellot G6,7,8.

Author information

1
Department of Genetics, Harvard Medical School, Boston, MA, 02115, USA.
2
Wyss Institute for Biologically Inspired Engineering, Harvard University, Boston, MA, 02115, USA.
3
Sculpting Evolution Group, Media Lab, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA.
4
Department of Cancer Biology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA, 02115, USA.
5
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, 02115, USA.
6
Institut de Génomique Fonctionnelle, Centre National de la Recherche Scientifique, CNRS Unité Mixte de Recherche UMR 5203, Institut National de la Santé et de la Recherche Médicale, INSERM U1191, Montpellier, 34000, France. gaetan.bellot@igf.cnrs.fr.
7
Université de Montpellier, Montpellier, 34000, France. gaetan.bellot@igf.cnrs.fr.
8
Institut de Génomique Fonctionnelle, 141 rue de la Cardonille, Montpellier, Cedex 5, 34094, France. gaetan.bellot@igf.cnrs.fr.

Abstract

Thirty percent of the human proteome is composed of membrane proteins that can perform a wide range of cellular functions and communications. They represent the core of modern medicine as the targets of about 50 % of all prescription pharmaceuticals. However, elucidating the structure of membrane proteins has represented a constant challenge, even in the modern era. To date, only a few hundred high-resolution structural models of membrane proteins are available. This chapter describes the emergence of DNA nanotechnology as a powerful tool for the structural characterization of membrane protein using solution-state nuclear magnetic resonance (NMR) spectroscopy. Here, we detail the large-scale synthesis of detergent-resistant DNA nanotubes that can be assembled into a dilute liquid crystal to be used as a weak-alignment media in solution NMR structure determination of membrane proteins.

KEYWORDS:

DNA origami; Membrane protein; Nuclear magnetic resonance; Residual dipolar coupling; Structural biology

PMID:
27813010
DOI:
10.1007/978-1-4939-6454-3_14
[Indexed for MEDLINE]

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