Abstract by Lavender Hsien-Jun Lin

Personal Infomation

Presenter's Name

Lavender Hsien-Jun Lin



Degree Level




Abstract Infomation


Chemistry and Biochemistry

Faculty Advisor

John Price


Investigation of the effect of reduced synthesis and degradation on in vivo protein stability


As medicine and technology progress, the mortality rate has been greatly decreased.  However, longevity is not the only thing people are want from life. People want to live a full disease free life without the handicaps of age. Aging itself is then the next factor we need to overcome. It has been shown that calorie restriction slows down the aging process. Our lab had showed that the slowing down of dietary restriction (DR) is associated with the protein turnover rate in the cell. Protein folding not only contributes to protein turnover rate, but also directly impacts protein function and aggregation. Understanding the protein folding changes during aging and DR can help complete the story of how protein turnover effect (slowdown) aging.  We are building on previous work by Fitzgerald and Colleagues to measure folding stability in vivo, by modifying surface amino acids.  Here we show which amino acids are the best reporters and the change (difference) of protein folding free energies due to changes in aging rate.