{"id":{"repo_id":"mississippi","oai_identifier":"oai:egrove.olemiss.edu:etd-2288"},"canonical_url":"https://search.dev.ndltd.org/etd/mississippi/oai:egrove.olemiss.edu:etd-2288","repository":{"repo_id":"mississippi","name":"University of Mississippi","base_url":"https://egrove.olemiss.edu/do/oai/"},"display":{"title":"Investigation of Neural and Epithelial Cadherin Monomer Properties Using a Molecular Dynamics Approach","abstract":"Neural and epithelial cadherin are adhesion proteins intensely studied by our lab. Although the sequence, structure, and conformation are similar for the two cadherins, there are several physical properties that differ: dimerization affinity, dimerization kinetics, intermediate structure, and critical residues for dimerization. In the presence of calcium, cadherins are in equilibrium between monomeric and dimeric states, and the scope of this thesis focuses on monomeric cadherin. These molecular dynamics evaluations are based on the testing of specific hypotheses regarding the intramolecular interactions of neural and epithelial cadherin. We particularly focus on interactions involving critical residues at the N-terminus of the proteins, the hydrophobic core residues, and the ionic surface area.","abstract_html":"Neural and epithelial cadherin are adhesion proteins intensely studied by our lab. Although the sequence, structure, and conformation are similar for the two cadherins, there are several physical properties that differ: dimerization affinity, dimerization kinetics, intermediate structure, and critical residues for dimerization. In the presence of calcium, cadherins are in equilibrium between monomeric and dimeric states, and the scope of this thesis focuses on monomeric cadherin. These molecular dynamics evaluations are based on the testing of specific hypotheses regarding the intramolecular interactions of neural and epithelial cadherin. We particularly focus on interactions involving critical residues at the N-terminus of the proteins, the hydrophobic core residues, and the ionic surface area.","abstract_has_math":false,"creators":["Fan, Lianyi"],"institution":null,"degree_name":"M.S. in Chemistry","degree_level":"Thesis","degree_discipline":"Chemistry and Biochemistry","degree_department":null,"school":null,"contributors":["Susan Pedigo","Michael Mossing","Robert J. Doerksen"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2016,"date_issued":"2016-01-01T08:00:00Z","date_published":"2016-01-01T08:00:00Z","updated_at":"2026-07-24T03:06:44Z","subjects":["Chemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://egrove.olemiss.edu/etd/1289","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Susan Pedigo","Michael Mossing","Robert J. 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Although the sequence, structure, and conformation are similar for the two cadherins, there are several physical properties that differ: dimerization affinity, dimerization kinetics, intermediate structure, and critical residues for dimerization. In the presence of calcium, cadherins are in equilibrium between monomeric and dimeric states, and the scope of this thesis focuses on monomeric cadherin. These molecular dynamics evaluations are based on the testing of specific hypotheses regarding the intramolecular interactions of neural and epithelial cadherin. We particularly focus on interactions involving critical residues at the N-terminus of the proteins, the hydrophobic core residues, and the ionic surface area."]},{"key":"dc:title","label":"Title","values":["Investigation of Neural and Epithelial Cadherin Monomer Properties Using a Molecular Dynamics Approach"]}]}],"canonical_facts":{"dc:contributor":["Susan Pedigo","Michael Mossing","Robert J. Doerksen"],"dc:creator":["Fan, Lianyi"],"dc:date.available":["2020-01-23T08:00:00Z"],"dc:description.abstract":["Neural and epithelial cadherin are adhesion proteins intensely studied by our lab. Although the sequence, structure, and conformation are similar for the two cadherins, there are several physical properties that differ: dimerization affinity, dimerization kinetics, intermediate structure, and critical residues for dimerization. In the presence of calcium, cadherins are in equilibrium between monomeric and dimeric states, and the scope of this thesis focuses on monomeric cadherin. These molecular dynamics evaluations are based on the testing of specific hypotheses regarding the intramolecular interactions of neural and epithelial cadherin. We particularly focus on interactions involving critical residues at the N-terminus of the proteins, the hydrophobic core residues, and the ionic surface area."],"dc:identifier":["https://egrove.olemiss.edu/etd/1289"],"dc:subject":["Chemistry"],"dc:title":["Investigation of Neural and Epithelial Cadherin Monomer Properties Using a Molecular Dynamics Approach"],"thesis:degree_discipline":["Chemistry and Biochemistry"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["M.S. in Chemistry"]},"updated_at":"2026-07-24T03:06:44Z"}