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dc.contributor.advisorGabriela Schlau-Cohen.en_US
dc.contributor.authorTong, Ashley(Ashley Lynn)en_US
dc.contributor.otherMassachusetts Institute of Technology. Department of Chemistry.en_US
dc.date.accessioned2020-03-09T18:51:22Z
dc.date.available2020-03-09T18:51:22Z
dc.date.copyright2019en_US
dc.date.issued2019en_US
dc.identifier.urihttps://hdl.handle.net/1721.1/124055
dc.descriptionThesis: Ph. D., Massachusetts Institute of Technology, Department of Chemistry, 2019en_US
dc.descriptionCataloged from PDF version of thesis.en_US
dc.descriptionIncludes bibliographical references (pages 67-79).en_US
dc.description.abstractUsing a unique approach to solar energy conversion, photosynthetic organisms have developed a light-harvesting process with near unity quantum efficiency. Light-harvesting proteins transfer energy from the sun to reach a central location, the reaction center, where charge separation occurs and energy is converted to chemical energy. Moreover, these proteins are able to carry out this efficient transfer in cellular membranes despite the complex environment found in these membranes. Particularly, light-harvesting in photosynthetic purple bacteria uses a diverse set of tools from species to species to efficiently transfer energy through this protein network. Induced by their habitats, external environmental pressures on the fitness of purple bacteria have caused species to evolve different mechanisms in order to deal with thesel pressures. Although these complexes have been studied for some time, there is still very little known about particular species.en_US
dc.description.abstractAdditionally, most previous work has been on non-native samples, such as detergent solubilized proteins, or on complex membranes such as vesicles, chromatophores, or whole membranes that contain multiple proteins with multiple processes occurring simultaneously. This work investigates how photosynthetic light-harvesting complexes are able to achieve their impressive efficiency using ensemble ultrafast spectroscopy to measure energy transfer dynamics and near-native discoidal model membrane-discs. These model membrane-discs provide a controlled environment to effectively study how energy is transferred in a single protein and between particular sets of proteins, allowing individual steps in the light-harvesting process to be probed without other processes interfering. They also provide a near-native system to explore how lipid-protein and protein-protein interactions affect the energy transfer kinetics in these proteins.en_US
dc.description.abstractAdditionally, this work explores the differences in energy transfer kinetics of light-harvesting proteins between species of purple bacteria. Overall, this provides new insights into the role the membrane plays in light-harvesting and how the composition of proteins within the native membrane of different species of purple bacteria can add variation to energy transfer kinetics.en_US
dc.description.statementofresponsibilityby Ashley Tong.en_US
dc.format.extent79 pagesen_US
dc.language.isoengen_US
dc.publisherMassachusetts Institute of Technologyen_US
dc.rightsMIT theses are protected by copyright. They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission.en_US
dc.rights.urihttp://dspace.mit.edu/handle/1721.1/7582en_US
dc.subjectChemistry.en_US
dc.titleA comparative look at structure-function roles in light-harvesting dynamics of purple bacteriaen_US
dc.typeThesisen_US
dc.description.degreePh. D.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistryen_US
dc.identifier.oclc1142099842en_US
dc.description.collectionPh.D. Massachusetts Institute of Technology, Department of Chemistryen_US
dspace.imported2020-03-09T18:51:22Zen_US
mit.thesis.degreeDoctoralen_US
mit.thesis.departmentChemen_US


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