{"id":{"repo_id":"columbia-diss","oai_identifier":"oai:academiccommons.columbia.edu:10.7916/D83B66HW"},"canonical_url":"https://search.dev.ndltd.org/etd/columbia-diss/oai:academiccommons.columbia.edu:10.7916/D83B66HW","repository":{"repo_id":"columbia-diss","name":"Columbia University","base_url":"https://academiccommons.columbia.edu/oai"},"display":{"title":"Gates and Latches: the mechanochemistry of ATP binding in kinesin 1 and Eg5","abstract":"This thesis explores the role of mechanochemistry in two biological systems. The first system investigated involves cargo transport along microtubule filaments by Kinesin 1. A gating mechanism is needed to coordinate ATP binding to the two catalytic domains within Kinesin 1 in order to prevent simultaneous binding, hydrolysis and detachment of both heads which could prematurely terminate cargo transport. The second system investigated involves cell division and the mitotic kinesin Eg5. In this motor, we investigate ATP-binding and find that it has an additional component internal to its catalytic domain, called Loop 5, which is functionally important for both ATP binding and neck linker docking.","abstract_html":"This thesis explores the role of mechanochemistry in two biological systems. The first system investigated involves cargo transport along microtubule filaments by Kinesin 1. A gating mechanism is needed to coordinate ATP binding to the two catalytic domains within Kinesin 1 in order to prevent simultaneous binding, hydrolysis and detachment of both heads which could prematurely terminate cargo transport. The second system investigated involves cell division and the mitotic kinesin Eg5. In this motor, we investigate ATP-binding and find that it has an additional component internal to its catalytic domain, called Loop 5, which is functionally important for both ATP binding and neck linker docking.","abstract_has_math":false,"creators":["Behnke-Parks, William M."],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011","date_published":"2011","updated_at":"2026-07-24T01:44:34Z","subjects":["Biology","Biophysics","Biochemistry","Kinesin","Mechanical chemistry","Cell division"],"languages":["English"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://doi.org/10.7916/D83B66HW","outbound_label":"DOI","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Behnke-Parks, William M."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011"]},{"key":"dc:type","label":"Dc Type","values":["Theses"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biology","Biophysics","Biochemistry","Kinesin","Mechanical chemistry","Cell division"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://doi.org/10.7916/D83B66HW"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["This thesis explores the role of mechanochemistry in two biological systems. The first system investigated involves cargo transport along microtubule filaments by Kinesin 1. A gating mechanism is needed to coordinate ATP binding to the two catalytic domains within Kinesin 1 in order to prevent simultaneous binding, hydrolysis and detachment of both heads which could prematurely terminate cargo transport. The second system investigated involves cell division and the mitotic kinesin Eg5. In this motor, we investigate ATP-binding and find that it has an additional component internal to its catalytic domain, called Loop 5, which is functionally important for both ATP binding and neck linker docking."]},{"key":"dc:title","label":"Title","values":["Gates and Latches: the mechanochemistry of ATP binding in kinesin 1 and Eg5"]}]}],"canonical_facts":{"dc:creator":["Behnke-Parks, William M."],"dc:date":["2011"],"dc:description":["This thesis explores the role of mechanochemistry in two biological systems. The first system investigated involves cargo transport along microtubule filaments by Kinesin 1. A gating mechanism is needed to coordinate ATP binding to the two catalytic domains within Kinesin 1 in order to prevent simultaneous binding, hydrolysis and detachment of both heads which could prematurely terminate cargo transport. The second system investigated involves cell division and the mitotic kinesin Eg5. In this motor, we investigate ATP-binding and find that it has an additional component internal to its catalytic domain, called Loop 5, which is functionally important for both ATP binding and neck linker docking."],"dc:identifier":["https://doi.org/10.7916/D83B66HW"],"dc:language":["English"],"dc:subject":["Biology","Biophysics","Biochemistry","Kinesin","Mechanical chemistry","Cell division"],"dc:title":["Gates and Latches: the mechanochemistry of ATP binding in kinesin 1 and Eg5"],"dc:type":["Theses"]},"updated_at":"2026-07-24T01:44:34Z"}