BYU

Abstract by Nathan Zuniga

Personal Infomation


Presenter's Name

Nathan Zuniga

Co-Presenters

None

Degree Level

Undergraduate

Co-Authors

John Price

Abstract Infomation


Department

Chemistry and Biochemistry

Faculty Advisor

John Price

Title

Detection of Post-Translational Modifications Using Mass Spectrometry

Abstract

Post-translational modifications affect protein mechanisms and are on occasion the cause of disease. Thus, it is important to create diagnostic methods that can detect modified proteins in the proteome. Proteomic studies performed on serum samples from Rheumatoid Arthritis patients indicate distinctions in protein melting curves, compared to the group of “healthy” individuals. These results potentially indicate protein modifications at positions in the amino acid (AA) sequence, including AAs that are not available for modification. Modifications were introduced at different folding stages, and Mass Spectrometry (MS) was used as a method to identify protein modification. Along with the protein denaturation curves, we are researching methods to used MS as a diagnostic method to detect detrimental protein modifications that lead to proteome-related disease.