Endoglucanases play a key role in the industrial production of bioethanol, but the most efficient method requires the utilization of high temperatures and is currently limited by the thermostability of endoglucanases. For this reason, it would be beneficial to discover more high-efficiency, thermostable enzymes to utilize in the hydrolytic process. In this study molecular dynamics simulations were performed on structurally similar endoglucanases with varying levels of thermostability to gain insight on what factors contribute to thermostability in endoglucanases. RMSD, RMSF, PCA, hydrogen bonding and salt bridges were analyzed. Finally, protein energy networks were constructed from nonbonded interaction potentials and analysis was performed using hub population, cluster population, largest community transition profiles and LCC profiles. It was found that the more thermostable endoglucanases exhibited a greater number of hydrogen bonds along with fewer, more segregated electrostatic interactions and a larger network of low-energy van der Waals interactions – likely responsible for providing adequate rigidity to withstand high-temperature conditions while still allowing the flexibility needed for proper catalytic function.
","abstract_html":"<p>Endoglucanases play a key role in the industrial production of bioethanol, but the most efficient method requires the utilization of high temperatures and is currently limited by the thermostability of endoglucanases. For this reason, it would be beneficial to discover more high-efficiency, thermostable enzymes to utilize in the hydrolytic process. In this study molecular dynamics simulations were performed on structurally similar endoglucanases with varying levels of thermostability to gain insight on what factors contribute to thermostability in endoglucanases. RMSD, RMSF, PCA, hydrogen bonding and salt bridges were analyzed. Finally, protein energy networks were constructed from nonbonded interaction potentials and analysis was performed using hub population, cluster population, largest community transition profiles and LCC profiles. It was found that the more thermostable endoglucanases exhibited a greater number of hydrogen bonds along with fewer, more segregated electrostatic interactions and a larger network of low-energy van der Waals interactions – likely responsible for providing adequate rigidity to withstand high-temperature conditions while still allowing the flexibility needed for proper catalytic function.</p>","abstract_has_math":false,"creators":["Sheffield, Logan E."],"institution":null,"degree_name":"Master of Science - Biotechnology","degree_level":"Thesis","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":["Alexandra Martynova-Van Kley","James Briggs","Brian Barngrover"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2021,"date_issued":"2021-06-15T07:00:00Z","date_published":"2021-06-15T07:00:00Z","updated_at":"2026-07-24T04:30:37Z","subjects":["Molecular Dynamics","Endoglucanases","Simulations","Thermostability","Hyperthermophiles","Thermophilic","Biochemistry","Biotechnology","Molecular Biology","Other Biochemistry, Biophysics, and Structural Biology","Structural Biology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://scholarworks.sfasu.edu/etds/451","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Alexandra Martynova-Van Kley","James Briggs","Brian Barngrover"]},{"key":"dc:creator","label":"Author","values":["Sheffield, Logan E."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2021-08-23T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science - Biotechnology"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Molecular Dynamics","Endoglucanases","Simulations","Thermostability","Hyperthermophiles","Thermophilic","Biochemistry","Biotechnology","Molecular Biology","Other Biochemistry, Biophysics, and Structural Biology","Structural Biology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://scholarworks.sfasu.edu/etds/451"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Endoglucanases play a key role in the industrial production of bioethanol, but the most efficient method requires the utilization of high temperatures and is currently limited by the thermostability of endoglucanases. For this reason, it would be beneficial to discover more high-efficiency, thermostable enzymes to utilize in the hydrolytic process. In this study molecular dynamics simulations were performed on structurally similar endoglucanases with varying levels of thermostability to gain insight on what factors contribute to thermostability in endoglucanases. RMSD, RMSF, PCA, hydrogen bonding and salt bridges were analyzed. Finally, protein energy networks were constructed from nonbonded interaction potentials and analysis was performed using hub population, cluster population, largest community transition profiles and LCC profiles. It was found that the more thermostable endoglucanases exhibited a greater number of hydrogen bonds along with fewer, more segregated electrostatic interactions and a larger network of low-energy van der Waals interactions – likely responsible for providing adequate rigidity to withstand high-temperature conditions while still allowing the flexibility needed for proper catalytic function.
"]},{"key":"dc:title","label":"Title","values":["Molecular Dynamics Simulations Provide Insight into Stability of Hyperthermophilic Endoglucanases"]}]}],"canonical_facts":{"dc:contributor":["Alexandra Martynova-Van Kley","James Briggs","Brian Barngrover"],"dc:creator":["Sheffield, Logan E."],"dc:date.available":["2021-08-23T07:00:00Z"],"dc:description.abstract":["Endoglucanases play a key role in the industrial production of bioethanol, but the most efficient method requires the utilization of high temperatures and is currently limited by the thermostability of endoglucanases. For this reason, it would be beneficial to discover more high-efficiency, thermostable enzymes to utilize in the hydrolytic process. In this study molecular dynamics simulations were performed on structurally similar endoglucanases with varying levels of thermostability to gain insight on what factors contribute to thermostability in endoglucanases. RMSD, RMSF, PCA, hydrogen bonding and salt bridges were analyzed. Finally, protein energy networks were constructed from nonbonded interaction potentials and analysis was performed using hub population, cluster population, largest community transition profiles and LCC profiles. It was found that the more thermostable endoglucanases exhibited a greater number of hydrogen bonds along with fewer, more segregated electrostatic interactions and a larger network of low-energy van der Waals interactions – likely responsible for providing adequate rigidity to withstand high-temperature conditions while still allowing the flexibility needed for proper catalytic function.
"],"dc:identifier":["https://scholarworks.sfasu.edu/etds/451"],"dc:subject":["Molecular Dynamics","Endoglucanases","Simulations","Thermostability","Hyperthermophiles","Thermophilic","Biochemistry","Biotechnology","Molecular Biology","Other Biochemistry, Biophysics, and Structural Biology","Structural Biology"],"dc:title":["Molecular Dynamics Simulations Provide Insight into Stability of Hyperthermophilic Endoglucanases"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["Master of Science - Biotechnology"]},"updated_at":"2026-07-24T04:30:37Z"}