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Investigation Of The Thermodynamic Properties Of The Oligomerization Domain Of Heterogeneous Nuclear Ribonucleoprotein C, John P. O'Brien Iii
Investigation Of The Thermodynamic Properties Of The Oligomerization Domain Of Heterogeneous Nuclear Ribonucleoprotein C, John P. O'Brien Iii
Honors Theses
The heterogeneous nuclear ribonucleoprotein C (hnRNP C) performs a critical role in the processing of nascent pre-messenger ribonucleic acid (pre-mRNA) transcripts as they exit DNA polymerase II. As the pre-mRNA transcripts emerge from the polymerase complex, they are bound by hnRNP C only if its nucleotide (NT) chain is longer than a certain nucleotide length. If the chain is long enough and binding occurs, the nucleotide strand is exported and processed as mRNA, whereas if the length requirement is not met, the RNA sequence is directed along a pathway to become small nuclear RNA (snRNA). The functional form of hnRNP …
Ribonuclease A Modification Induced By 1,2-Naphthoquinone And 2-Hydroxy-1,4-Naphthoquinone, Michelle Dawn Smith
Ribonuclease A Modification Induced By 1,2-Naphthoquinone And 2-Hydroxy-1,4-Naphthoquinone, Michelle Dawn Smith
Honors Theses
Protein modifications may occur upon exposure to environmental toxins such as polycyclic aromatic hydrocarbon (PAH) molecules or their metabolites. In this context, our laboratory was interested in investigating protein modifications in the presence of select naphthoquinones, which were 2-hydroxy-1,4-naphthoquinone (HNQ) and 1,2-naphthoquinone (o-NQ). The effects of HNQ and o-NQ on the protein Ribonuclease A (RNase) were investigated through a variety of conditions. These modified incubation conditions included pH variation and the addition of metal ions to further mimic physiological conditions. Documentation of results was carried out through sodium dodecyl sulfate polyacrylamide gel electrophoretic analysis (SDS-PAGE). Of the two quinones, o-NQ …