Event Title

The Molecular Interaction Between c-KIT Receptor Protein (STI-571) and Threonine

Session Number

Project ID: CHEM 04

Advisor(s)

Dr. Joseph Golab, Illinois Mathematics and Science Academy

Discipline

Chemistry

Start Date

20-4-2022 9:10 AM

End Date

20-4-2022 9:25 AM

Abstract

STI-571’s role in the medical field is not as significant as other proteins, so we are interested in the logistics of its interaction with amino acids, such as Threonine. We applied the SPARTAN software to model the STI-571 molecule and Thr. We then made atomic substitutions, including changing a few Nitrogen atoms to Carbon atoms. Despite such changes, the distance between the Thr gatekeeping residue and the STI-571 protein stayed within 0.6 angstroms, suggesting that the molecule change did not make much of an effect on the distances of the model. When atoms farther away from Thr are changed, it has less impact on the length of the hydrogen bonding between the Oxygen on Thr and the Hydrogen on STI-571, but when it's closer, it has more impact. The changes made to the base case of the protein increased the overall energy change, indicating the atom change is not favorable for the orientation and structure of the protein. By modeling the STI-571 protein, we will not only have a better understanding of how such a protein functions but will also be able to discover more regarding its role in the treatment of certain cancers.

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Apr 20th, 9:10 AM Apr 20th, 9:25 AM

The Molecular Interaction Between c-KIT Receptor Protein (STI-571) and Threonine

STI-571’s role in the medical field is not as significant as other proteins, so we are interested in the logistics of its interaction with amino acids, such as Threonine. We applied the SPARTAN software to model the STI-571 molecule and Thr. We then made atomic substitutions, including changing a few Nitrogen atoms to Carbon atoms. Despite such changes, the distance between the Thr gatekeeping residue and the STI-571 protein stayed within 0.6 angstroms, suggesting that the molecule change did not make much of an effect on the distances of the model. When atoms farther away from Thr are changed, it has less impact on the length of the hydrogen bonding between the Oxygen on Thr and the Hydrogen on STI-571, but when it's closer, it has more impact. The changes made to the base case of the protein increased the overall energy change, indicating the atom change is not favorable for the orientation and structure of the protein. By modeling the STI-571 protein, we will not only have a better understanding of how such a protein functions but will also be able to discover more regarding its role in the treatment of certain cancers.