Abstract by Ji Sun Stella Park

Personal Infomation

Presenter's Name

Ji Sun Stella Park

Degree Level



Hsien Jung Lavender Lin
Nathan Zuniga
Kim Wagstaff
John Price

Abstract Infomation


Chemistry and Biochemistry

Faculty Advisor

J.C. Price


Optimizing a proteome scale measurement of protein fold stability


Aging is directly related to the homeostasis of proteins (proteostasis), where loss of proteostasis becomes more profound as we age. We want to measure the the protein structural stability for every protein in the proteome as a metric of in vivo quality. This assay can be used to compare the stability and quality of abnormally functioning proteins identify changes that occur as we lose proteostasis. Our method consists of covalent modification of proteins during a denaturation curve. The midpoint, where the ratio between folded and denatured protein is at 1:1 reports the stability of each protein.  We expect that the stability will change as proteostasis control fails during aging. We tested different amino acid modifiers during denaturation to compare the labeling efficiency on the amino acids. The results of these tests are compared to identify an optimal labeling method that efficiently and reproducibly measured amino acid accessibility and accurately reported protein fold stability.