Striated Muscle UNC-45, also known as UNC-45b, is an important protein that acts as a chaperone for myosin in cardiac and skeletal muscles, binding to myosin at its C-terminal UCS domain and regulating its assembly into thick filaments and sarcomeric structures. The UCS domain contains a large loop that is believed to be the first point of interaction between myosin and UNC-45b. GATA-4 is an essential transcription factor that facilitates transcription of several genes in cardiac development, particularly alpha-heavy chain myosin in heart tissue. Recently, studies have shown that there is interaction of GATA-4 with UNC-45b and that GATA-4 binds to the UCS domain. The implications of this interaction suggests that UNC-45b may play a role in not only the folding of myosin, but in the transcription of it as well. The aim of this study was to identify potential interaction interfaces between GATA-4 and the loop of UNC-45b and determine if the interactions are specific through computational models. Computational analysis suggests that the UCS loop is the preferential binding site of GATA-4 and that van der Waals packing is the primary method of binding.
","abstract_html":"<p> Striated Muscle UNC-45, also known as UNC-45b, is an important protein that acts as a chaperone for myosin in cardiac and skeletal muscles, binding to myosin at its C-terminal UCS domain and regulating its assembly into thick filaments and sarcomeric structures. The UCS domain contains a large loop that is believed to be the first point of interaction between myosin and UNC-45b. GATA-4 is an essential transcription factor that facilitates transcription of several genes in cardiac development, particularly alpha-heavy chain myosin in heart tissue. Recently, studies have shown that there is interaction of GATA-4 with UNC-45b and that GATA-4 binds to the UCS domain. The implications of this interaction suggests that UNC-45b may play a role in not only the folding of myosin, but in the transcription of it as well. The aim of this study was to identify potential interaction interfaces between GATA-4 and the loop of UNC-45b and determine if the interactions are specific through computational models. Computational analysis suggests that the UCS loop is the preferential binding site of GATA-4 and that van der Waals packing is the primary method of binding.</p>","abstract_has_math":false,"creators":["Duncan, Drake Alexander"],"institution":null,"degree_name":"Master of Science in Natural Science","degree_level":"Thesis","degree_discipline":"Chemistry and Biochemistry","degree_department":null,"school":null,"contributors":["Dr. Odutayo Odunuga","Dr. Darrell Fry","Dr. Michele Harris"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2021,"date_issued":"2021-05-01T07:00:00Z","date_published":"2021-05-01T07:00:00Z","updated_at":"2026-07-24T04:30:30Z","subjects":["UNC-45","GATA-4","bioinformatics","UCS","chaperone","transcription factor","interaction","Biochemistry","Chemistry","Molecular Biology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://scholarworks.sfasu.edu/etds/371","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Dr. Odutayo Odunuga","Dr. Darrell Fry","Dr. Michele Harris"]},{"key":"dc:creator","label":"Author","values":["Duncan, Drake Alexander"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2021-05-06T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry and Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science in Natural Science"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["UNC-45","GATA-4","bioinformatics","UCS","chaperone","transcription factor","interaction","Biochemistry","Chemistry","Molecular Biology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://scholarworks.sfasu.edu/etds/371"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Striated Muscle UNC-45, also known as UNC-45b, is an important protein that acts as a chaperone for myosin in cardiac and skeletal muscles, binding to myosin at its C-terminal UCS domain and regulating its assembly into thick filaments and sarcomeric structures. The UCS domain contains a large loop that is believed to be the first point of interaction between myosin and UNC-45b. GATA-4 is an essential transcription factor that facilitates transcription of several genes in cardiac development, particularly alpha-heavy chain myosin in heart tissue. Recently, studies have shown that there is interaction of GATA-4 with UNC-45b and that GATA-4 binds to the UCS domain. The implications of this interaction suggests that UNC-45b may play a role in not only the folding of myosin, but in the transcription of it as well. The aim of this study was to identify potential interaction interfaces between GATA-4 and the loop of UNC-45b and determine if the interactions are specific through computational models. Computational analysis suggests that the UCS loop is the preferential binding site of GATA-4 and that van der Waals packing is the primary method of binding.
"]},{"key":"dc:title","label":"Title","values":["Simulation of the Interaction Between Striated Muscle UNC-45 and Transcription Factor GATA-4"]}]}],"canonical_facts":{"dc:contributor":["Dr. Odutayo Odunuga","Dr. Darrell Fry","Dr. Michele Harris"],"dc:creator":["Duncan, Drake Alexander"],"dc:date.available":["2021-05-06T07:00:00Z"],"dc:description.abstract":["Striated Muscle UNC-45, also known as UNC-45b, is an important protein that acts as a chaperone for myosin in cardiac and skeletal muscles, binding to myosin at its C-terminal UCS domain and regulating its assembly into thick filaments and sarcomeric structures. The UCS domain contains a large loop that is believed to be the first point of interaction between myosin and UNC-45b. GATA-4 is an essential transcription factor that facilitates transcription of several genes in cardiac development, particularly alpha-heavy chain myosin in heart tissue. Recently, studies have shown that there is interaction of GATA-4 with UNC-45b and that GATA-4 binds to the UCS domain. The implications of this interaction suggests that UNC-45b may play a role in not only the folding of myosin, but in the transcription of it as well. The aim of this study was to identify potential interaction interfaces between GATA-4 and the loop of UNC-45b and determine if the interactions are specific through computational models. Computational analysis suggests that the UCS loop is the preferential binding site of GATA-4 and that van der Waals packing is the primary method of binding.
"],"dc:identifier":["https://scholarworks.sfasu.edu/etds/371"],"dc:subject":["UNC-45","GATA-4","bioinformatics","UCS","chaperone","transcription factor","interaction","Biochemistry","Chemistry","Molecular Biology"],"dc:title":["Simulation of the Interaction Between Striated Muscle UNC-45 and Transcription Factor GATA-4"],"thesis:degree_discipline":["Chemistry and Biochemistry"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["Master of Science in Natural Science"]},"updated_at":"2026-07-24T04:30:30Z"}