Honors Theses
Date of Award
Winter 12-13-2025
Document Type
Undergraduate Thesis
Department
Chemistry and Biochemistry
First Advisor
Sujay Ray
Second Advisor
Saumen Chakraborty
Third Advisor
Wayne Gray
Relational Format
Dissertation/Thesis
Abstract
Many remarkable discoveries, especially in the last decade, have shown scientists just how important RNA is. In this study, the secondary structure of RNA, G-Quadruplexes, is the topic of interest and how they are affected by salts and S1 protein. To obtain the S1 protein it was transformed from E. Coli using a bacterial plasmid. The S1 protein was then purified from the bacteria through the use of many purification methods. The monovalent cationic salts used were LiCl and KCl which have different ionic radii size that contributes to the stability of RNA G-Quadruplexes. This stability was observed and affected the folding of the G-Quadruplexes. To observe the relationship of the salts on the quadruplexes a Native-PAGE gel was run using differing concentrations of the salts. The Native-Page gels were also used to see how the salts and S1 affect RNA G-Quadruplex folding. As the amount of KCl increased so did the amount of quadruplex folding as the top band faded and the bottom band intensified on the gel. This was also seen with LiCl. Then a 500mM concentration of salts were each run with an increasing concentration of S1 to see how it affects the quadruplex folding. From the gels, it can be seen that as the concentration of S1 increases so does the amount of S1 bound to RNA prohibiting the formation of quadruplexes and unwinding that secondary structure. Through this data it can be concluded that the KCl stabilizes the G-Quadruplex and the S1 protein unfolds the quadruplex as it binds to the RNA.
Recommended Citation
Martin, Chloe M., "The Dynamic Interplay between Monovalent Salts and Ribosomal Protein S1 in Regulating RNA G-Quadruplex Structure" (2025). Honors Theses. 3364.
https://egrove.olemiss.edu/hon_thesis/3364
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