A closer look at serine’s structure and function in serine protease

The purpose of analyzing serine in serine protease is to understand how this enzyme impacts the hydrolysis of proteins. To analyze and compute calculations with serine, first principle electronic structure calculations were utilized. The electrostatic potential maps for an optimized serine molecule were determined. Additionally, the active site of the serine protease trypsin was studied to determine if the generally accepted mechanism where serine is deprotonated by histidine can be supported by density functional theory (DFT). Trypsin is an enzyme made in the pancreas and released into the small intestine. Serine was modeled in its zwitterion form because the pH of these two organs ranges from neutral to basic. Overall, these calculations have further clarified the structure and chemical properties of serine in trypsin, providing an enhanced understanding of the potential reactions catalyzed by serine proteases.

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Work Title A closer look at serine’s structure and function in serine protease
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Open Access
Creators
  1. Lauren Conrad
  2. Lorena Tribe
Keyword
  1. Serine
  2. Density Functional Theory
  3. Protease
  4. Computational Chemistry
License CC BY 4.0 (Attribution)
Work Type Poster
Publication Date April 2023
DOI doi:10.26207/a656-vt73
Deposited April 27, 2023

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Version 1
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  • Updated
  • Updated Acknowledgments Show Changes
    Acknowledgments
    • Faculty advisor: Dr. Lorena Tribe
  • Added Creator Lauren Conrad
  • Added ConradLauren_ACSPoster_URA23.pdf
  • Updated License Show Changes
    License
    • https://creativecommons.org/licenses/by/4.0/
  • Published
  • Updated Acknowledgments Show Changes
    Acknowledgments
    • Faculty advisor: Dr. Lorena Tribe
  • Added Creator Lorena Tribe
  • Updated