Liquid Crystalline Phase of G-Tetrad DNA for NMR Study of Detergent-Solubilized Protein

Ad Bax (1235142)

Justin Lorieau (1264587)

Lishan Yao (430891)

Structure determination of membrane proteins remains an important but difficult research target. Solution NMR offers a number of experimentally accessible parameters that can aid in structural studies, including interproton distances derived from NOEs, torsion angles from J-couplings and chemical shift data, and vector orientations from residual dipolar couplings (RDCs).1,2 RDCs constrain the orientations of internuclear vectors relative to a molecular axis system and therefore carry information that is inherently global in character. RDCs in solution result from an anisotropic distribution of molecular orientations in the sample. Such anisotropy can be introduced by adding a low volume fraction of nematogens to the aqueous solvent, which align in a liquid crystalline (LC) manner relative to an external strong magnetic field. Alternatively, weak macromolecular order can be induced by dissolving the protein in a highly hydrated, anisotropically com

Justin Lorieau

Lishan Yao

Ad Bax

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A (2008) Liquid Crystalline Phase of G-Tetrad DNA for NMR Study of Detergent-Solubilized Proteins

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Liquid Crystalline Phase of G-Tetrad DNA for NMR Study of Detergent-Solubilized Proteins

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Liquid Crystalline Phase of G-Tetrad DNA for NMR Study of Detergent-Solubilized Proteins

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