Biomedical Engineering Reference
In-Depth Information
Chapter 16
DNA-Nanotube-Enabled NMR Structure
Determination of Membrane Proteins
John Min, William M. Shih, and Gaetan Bellot
Abstract
One of the most fundamental questions in cell biology concerns how
membrane proteins can perform or contribute to cell communication. Over the
last few decades, we have seen major advances in understanding the struc-
tural mechanisms of membrane proteins. This chapter describes the emergence
of DNA nanotechnology as a powerful tool for the structural characterization
of membrane-associated protein using solution-state nuclear magnetic resonance
(NMR) spectroscopy. Solution-state NMR is currently one of the best known
methods for studying membrane protein structure, and a residual dipolar coupling-
based refinement approach can be used to solve the structure of membrane proteins
up to 40 kDa in size. However, a weak-alignment medium that is detergent-resistant
is required. Previously, availability of media suitable for inducing weak alignment
of membrane proteins was severely limited. Recently, in the William Shih's group,
we introduced a large-scale synthesis of detergent-resistant DNA nanotubes that
can be assembled into dilute liquid crystals for application as weak-alignment
media in solution NMR structure determination of membrane proteins. Nanotube-
based alignment of membrane proteins represents a fine example of the productive
interface between DNA nanotechnology and structural biology.
Keywords
DNA origami • Nuclear magnetic resonance • Structural biology •
Membrane protein •
Protein structure determination •
DNA liquid crystal
•
Residual dipolar coupling
J. Min • W.M. Shih • G. Bellot (
)
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School,
Boston, MA 02115, USA
Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02115, USA
Wyss Institute for Biologically Inspired Engineering at Harvard, Cambridge, MA 02138, USA
e-mail:
Bellot.gaetan@gmail.com
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