{"id":{"repo_id":"baylor","oai_identifier":"oai:baylor-ir.tdl.org:2104/13922"},"canonical_url":"https://search.dev.ndltd.org/etd/baylor/oai:baylor-ir.tdl.org:2104/13922","repository":{"repo_id":"baylor","name":"Baylor University","base_url":"https://baylor-ir.tdl.org/server/oai/request"},"display":{"title":"Exploring SOD1 electron transfer, heterodimerization, and hetero-amyloid formation.","abstract":"Cu, Zn Superoxide dismutase (SOD1) is an essential metalloenzyme that regulates superoxide radicals. Because SOD1 is a long-lived protein, it contains an intrinsic molecular clock, deamidation, that accumulates over time. Misfolding and aggregation of SOD1 have been linked to neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and, more recently, Parkinson's disease. To investigate the molecular factors underlying these processes, this dissertation examines the protein from the inside out, focusing on three concepts: (i) the metal center, (ii) subunit swapping, and (iii) hetero-amyloid formation. In chapter two, I use an analytical method, “protein charge ladders”, to distinguish between electron transfer (ET) and proton-coupled electron transfer (PCET) in a binuclear copper center by directly measuring the change in protein net charge upon reduction/oxidation (ΔZ4ET). Chapter three explores a hyper-deamidated form of SOD1, containing five of the protein’s seven deamidations, and evaluates how this natural post-translational modification affects heterodimerization. Chapter four investigates how the aggregation propensity of WT is altered in the presence of two mutations that do not aggregate in vitro.","abstract_html":"Cu, Zn Superoxide dismutase (SOD1) is an essential metalloenzyme that regulates superoxide radicals. Because SOD1 is a long-lived protein, it contains an intrinsic molecular clock, deamidation, that accumulates over time. Misfolding and aggregation of SOD1 have been linked to neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and, more recently, Parkinson's disease. To investigate the molecular factors underlying these processes, this dissertation examines the protein from the inside out, focusing on three concepts: (i) the metal center, (ii) subunit swapping, and (iii) hetero-amyloid formation. In chapter two, I use an analytical method, “protein charge ladders”, to distinguish between electron transfer (ET) and proton-coupled electron transfer (PCET) in a binuclear copper center by directly measuring the change in protein net charge upon reduction/oxidation (ΔZ4ET). Chapter three explores a hyper-deamidated form of SOD1, containing five of the protein’s seven deamidations, and evaluates how this natural post-translational modification affects heterodimerization. Chapter four investigates how the aggregation propensity of WT is altered in the presence of two mutations that do not aggregate in vitro.","abstract_has_math":false,"creators":["Gonzalez, Mayte, 1998-"],"institution":"Baylor University.","degree_name":"Ph.D.","degree_level":"Doctoral","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Shaw, Bryan Francis, 1976-"],"committee_chairs":[],"committee_members":[],"year":2025,"date_issued":"2025-08","date_published":"2025-08","updated_at":"2026-07-24T01:08:13Z","subjects":["Superoxide dismutase (SOD1)","Charge regulation.","Proton-coupled electron transfer (PCET)","Heterodimerization.","Deamidation.","Amyloid formation."],"languages":["en"],"rights":["Baylor University works are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. 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To investigate the molecular factors underlying these processes, this dissertation examines the protein from the inside out, focusing on three concepts: (i) the metal center, (ii) subunit swapping, and (iii) hetero-amyloid formation. In chapter two, I use an analytical method, “protein charge ladders”, to distinguish between electron transfer (ET) and proton-coupled electron transfer (PCET) in a binuclear copper center by directly measuring the change in protein net charge upon reduction/oxidation (ΔZ4ET). Chapter three explores a hyper-deamidated form of SOD1, containing five of the protein’s seven deamidations, and evaluates how this natural post-translational modification affects heterodimerization. Chapter four investigates how the aggregation propensity of WT is altered in the presence of two mutations that do not aggregate in vitro."]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Exploring SOD1 electron transfer, heterodimerization, and hetero-amyloid formation."]}]}],"canonical_facts":{"dc:contributor.advisor":["Shaw, Bryan Francis, 1976-"],"dc:creator":["Gonzalez, Mayte, 1998-"],"dc:date.accessioned":["2025-09-19T02:28:52Z"],"dc:date.issued":["2025-08"],"dc:description.abstract":["Cu, Zn Superoxide dismutase (SOD1) is an essential metalloenzyme that regulates superoxide radicals. Because SOD1 is a long-lived protein, it contains an intrinsic molecular clock, deamidation, that accumulates over time. Misfolding and aggregation of SOD1 have been linked to neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and, more recently, Parkinson's disease. To investigate the molecular factors underlying these processes, this dissertation examines the protein from the inside out, focusing on three concepts: (i) the metal center, (ii) subunit swapping, and (iii) hetero-amyloid formation. In chapter two, I use an analytical method, “protein charge ladders”, to distinguish between electron transfer (ET) and proton-coupled electron transfer (PCET) in a binuclear copper center by directly measuring the change in protein net charge upon reduction/oxidation (ΔZ4ET). Chapter three explores a hyper-deamidated form of SOD1, containing five of the protein’s seven deamidations, and evaluates how this natural post-translational modification affects heterodimerization. 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