{"id":{"repo_id":"baylor","oai_identifier":"oai:baylor-ir.tdl.org:2104/12960"},"canonical_url":"https://search.dev.ndltd.org/etd/baylor/oai:baylor-ir.tdl.org:2104/12960","repository":{"repo_id":"baylor","name":"Baylor University","base_url":"https://baylor-ir.tdl.org/server/oai/request"},"display":{"title":"Overcoming barriers in chemistry : a birds eye view of electrostatic fluctuations in fundamental proteins and streamlining inclusivity in the classroom.","abstract":"Electrostatic interactions play an important role in protein biochemistry. The net charge of a protein (Z) can influence the structure, function, and solubility but is often overlooked in classical biochemistry. In Chapter two, I investigate the ability of a Rieske Iron-Sulfur (ISP) metalloprotein to accept an electron with varying pH (5.5 – 10.6) and the effect this electron transfer has on the overall net charge. Additionally, the trends in the Rieske ISP's Z and ∆ZET are explored as well as the ∆ZET and protonation free energy (∆∆GH+) over pH. In Chapter Three, I selectively crosslinked a model enzyme, RNase A to three differently charged protein crowders at a distance below the Debye length (≤ 7.9 Å) to determine how the net charge of the crowder affects the enzymatic activity of the enzyme. Chapter four is dedicated to a project that improves the inclusivity of the blind and visually impaired in the classroom by 3D printing common science data using an ancient art form known as the lithophane that can be interpreted with the same level of detail by both the blind and sighted.","abstract_html":"Electrostatic interactions play an important role in protein biochemistry. The net charge of a protein (Z) can influence the structure, function, and solubility but is often overlooked in classical biochemistry. In Chapter two, I investigate the ability of a Rieske Iron-Sulfur (ISP) metalloprotein to accept an electron with varying pH (5.5 – 10.6) and the effect this electron transfer has on the overall net charge. Additionally, the trends in the Rieske ISP's Z and ∆ZET are explored as well as the ∆ZET and protonation free energy (∆∆GH+) over pH. In Chapter Three, I selectively crosslinked a model enzyme, RNase A to three differently charged protein crowders at a distance below the Debye length (≤ 7.9 Å) to determine how the net charge of the crowder affects the enzymatic activity of the enzyme. Chapter four is dedicated to a project that improves the inclusivity of the blind and visually impaired in the classroom by 3D printing common science data using an ancient art form known as the lithophane that can be interpreted with the same level of detail by both the blind and sighted.","abstract_has_math":false,"creators":["Koone, Jordan C., 1996-"],"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":2024,"date_issued":"2024-05","date_published":"2024-05","updated_at":"2026-07-24T01:07:52Z","subjects":["Electrostatics.","Charge regulation.","Proton pump.","Rieske protein.","Cross linking.","Inclusivity.","Lithophane."],"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. Contact libraryquestions@baylor.edu for inquiries about permission."],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/2104/12960","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Shaw, Bryan Francis, 1976-"]},{"key":"dc:creator","label":"Author","values":["Koone, Jordan C., 1996-"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2024-09-13T13:19:46Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2024-09-13T13:19:46Z"]},{"key":"dc:date.issued","label":"Date","values":["2024-05"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Doctoral"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Baylor University."]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Electrostatics.","Charge regulation.","Proton pump.","Rieske protein.","Cross linking.","Inclusivity.","Lithophane."]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["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. Contact libraryquestions@baylor.edu for inquiries about permission."]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/2104/12960"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Electrostatic interactions play an important role in protein biochemistry. The net charge of a protein (Z) can influence the structure, function, and solubility but is often overlooked in classical biochemistry. In Chapter two, I investigate the ability of a Rieske Iron-Sulfur (ISP) metalloprotein to accept an electron with varying pH (5.5 – 10.6) and the effect this electron transfer has on the overall net charge. Additionally, the trends in the Rieske ISP's Z and ∆ZET are explored as well as the ∆ZET and protonation free energy (∆∆GH+) over pH. In Chapter Three, I selectively crosslinked a model enzyme, RNase A to three differently charged protein crowders at a distance below the Debye length (≤ 7.9 Å) to determine how the net charge of the crowder affects the enzymatic activity of the enzyme. Chapter four is dedicated to a project that improves the inclusivity of the blind and visually impaired in the classroom by 3D printing common science data using an ancient art form known as the lithophane that can be interpreted with the same level of detail by both the blind and sighted."]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Overcoming barriers in chemistry : a birds eye view of electrostatic fluctuations in fundamental proteins and streamlining inclusivity in the classroom."]}]}],"canonical_facts":{"dc:contributor.advisor":["Shaw, Bryan Francis, 1976-"],"dc:creator":["Koone, Jordan C., 1996-"],"dc:date.accessioned":["2024-09-13T13:19:46Z"],"dc:date.available":["2024-09-13T13:19:46Z"],"dc:date.issued":["2024-05"],"dc:description.abstract":["Electrostatic interactions play an important role in protein biochemistry. The net charge of a protein (Z) can influence the structure, function, and solubility but is often overlooked in classical biochemistry. In Chapter two, I investigate the ability of a Rieske Iron-Sulfur (ISP) metalloprotein to accept an electron with varying pH (5.5 – 10.6) and the effect this electron transfer has on the overall net charge. Additionally, the trends in the Rieske ISP's Z and ∆ZET are explored as well as the ∆ZET and protonation free energy (∆∆GH+) over pH. In Chapter Three, I selectively crosslinked a model enzyme, RNase A to three differently charged protein crowders at a distance below the Debye length (≤ 7.9 Å) to determine how the net charge of the crowder affects the enzymatic activity of the enzyme. Chapter four is dedicated to a project that improves the inclusivity of the blind and visually impaired in the classroom by 3D printing common science data using an ancient art form known as the lithophane that can be interpreted with the same level of detail by both the blind and sighted."],"dc:format.mimetype":["application/pdf"],"dc:identifier.uri":["https://hdl.handle.net/2104/12960"],"dc:language.iso":["en"],"dc: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. Contact libraryquestions@baylor.edu for inquiries about permission."],"dc:subject":["Electrostatics.","Charge regulation.","Proton pump.","Rieske protein.","Cross linking.","Inclusivity.","Lithophane."],"dc:title":["Overcoming barriers in chemistry : a birds eye view of electrostatic fluctuations in fundamental proteins and streamlining inclusivity in the classroom."],"dc:type":["Thesis"],"thesis:degree_level":["Doctoral"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["Baylor University."]},"updated_at":"2026-07-24T01:07:52Z"}