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Refinement of Loop Structure in Human Aquaporin-1 by Solid-State NMR Spectroscopy

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dc.contributor.advisor Ladizhansky, Vladimir
dc.contributor.advisor Brown, Leonid Dingwell, Dylan Archer 2019-05-30T15:09:16Z 2019-11-28T06:00:32Z 2019-05 2019-05-28 2019-05-30
dc.description.abstract Human aquaporin-1 (hAQP1) is a channel protein which selectively facilitates translocation of water across the cell membrane, serving important physiological functions including epithelial fluid transport in the renal system. Several crystal structures of hAQP1 have been determined at moderate resolution, but these structures broadly diverge in their representation of hAQP1’s long extracellular loop C, which may participate in functionally relevant interactions with the residues defining the protein’s central pore. This thesis investigates the structure of loop C at non-cryogenic temperature in a native-like lipid environment via MAS SSNMR spectroscopy. Selective recoupling through homogeneously broadened rotational resonance was applied in multidimensional correlation experiments in order to observe internuclear correlations involving loop C residues. The observed correlations provided sufficient distance restraints to develop a refined structural model of loop C using the molecular structure determination program Xplor-NIH. The refined model accounts for physiologically relevant interactions between the loop and the central pore. en_US
dc.language.iso en en_US
dc.rights Attribution-NoDerivatives 4.0 International *
dc.rights.uri *
dc.subject solid-state nmr en_US
dc.subject nmr en_US
dc.subject aquaporin en_US
dc.subject membrane proteins en_US
dc.title Refinement of Loop Structure in Human Aquaporin-1 by Solid-State NMR Spectroscopy en_US
dc.type Thesis en_US Biophysics en_US Master of Science en_US Department of Physics en_US
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