Molecular Dynamics Simulations Provide Insight into Stability of Hyperthermophilic Endoglucanases

Author

Logan E. Sheffield, Stephen F Austin State UniversityFollow

Date of Award

Summer 6-15-2021

Degree Type

Thesis

Degree Name

Master of Science - Biotechnology

Department

Biology

First Advisor

Alexandra Martynova-Van Kley

Second Advisor

James Briggs

Third Advisor

Brian Barngrover

Fourth Advisor

Lindsay Porter

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.

Repository Citation

Sheffield, Logan E., "Molecular Dynamics Simulations Provide Insight into Stability of Hyperthermophilic Endoglucanases" (2021). Electronic Theses and Dissertations. 451.
https://scholarworks.sfasu.edu/etds/451

Creative Commons License

This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.