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Identifying the Sugars and Phospholipids Tightly Bound to an Integral Membrane Protein

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dc.contributor.advisor Ladizhansky, Vladimir
dc.contributor.author de Vlugt, Jeffrey
dc.date.accessioned 2019-09-06T13:03:27Z
dc.date.available 2019-09-06T13:03:27Z
dc.date.copyright 2019-08
dc.date.created 2019-08-29
dc.date.issued 2019-09-06
dc.identifier.uri http://hdl.handle.net/10214/17386
dc.description.abstract Anabaena Sensory Rhodopsin (ASR) is a microbial photosensor found in cyanobacterium Anabaena sp. PCC 7120. It was found in previous studies that ASR co-purifies with several small molecules, although the identities and structural or functional roles remained unclear. In this thesis, two-dimensional and three-dimensional solid-state nuclear magnetic resonance (NMR) experiments and complementary methods were used to assign NMR signals of these molecules. The identified chemical shift patterns correspond to N-acetyl-D-glucosamine, N-acetyl-D-mannosaminuronic acid, 4-acetomido-4,6-dideoxy-D-galactose, and to a common phospholipid phosphatidylethanolamine (PE). The acyl tails of PE were identified based on characteristic product ion masses using liquid chromatography-mass spectrometry. Numerous correlations atypical for protein amino acids were found in the NMR spectra; they may result from PE acyl tails that are tightly bound by non-covalent interactions along the surface of transmembrane alpha-helices. The sugars likely feature a phospholipid aglycone that allows them to bind to ASR in a similar manner. en_US
dc.language.iso en en_US
dc.publisher University of Guelph en_US
dc.rights Attribution 4.0 International *
dc.rights.uri http://creativecommons.org/licenses/by/4.0/ *
dc.subject nuclear en_US
dc.subject magnetic en_US
dc.subject resonance en_US
dc.subject GlcNAc en_US
dc.subject Fuc4NAc en_US
dc.subject ManNAcA en_US
dc.subject solid-state NMR en_US
dc.subject solution NMR en_US
dc.subject 31P NMR en_US
dc.subject SSNMR en_US
dc.subject tightly-bound en_US
dc.subject co-purifies en_US
dc.subject ASR en_US
dc.subject anabaena en_US
dc.subject rhodopsin en_US
dc.subject constant-time en_US
dc.subject INEPT en_US
dc.subject TOBSY en_US
dc.subject DARR en_US
dc.subject CP en_US
dc.subject cross-polarization en_US
dc.subject insensitive nuclei enhanced by polarization transfer en_US
dc.subject phosphatidylethanolamine en_US
dc.subject PE en_US
dc.subject lipids en_US
dc.subject sugars en_US
dc.subject phospholipids en_US
dc.subject enterobacterial common antigen en_US
dc.subject ECA en_US
dc.subject integral en_US
dc.subject membrane en_US
dc.subject protein en_US
dc.subject E. coli en_US
dc.subject co-purification en_US
dc.title Identifying the Sugars and Phospholipids Tightly Bound to an Integral Membrane Protein en_US
dc.type Thesis en_US
dc.degree.programme Physics en_US
dc.degree.name Master of Science en_US
dc.degree.department Department of Physics en_US
dc.degree.grantor University of Guelph en_US


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