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PhD candidate Yvonne Chan a ‘protein engineer’

By Megan Bard and Tamm Bui

UMass Medical School Communications

August 07, 2017

As an undergraduate at Amherst College, Yvonne Chan was able design her own degree. Passionate about biology and fine arts, Chan earned a double major and now applies the disciplines to her studies as a PhD candidate at UMass Medical School.

“I’m fascinated by the complex set of reactions and interactions that must take place in the cell for survival and I integrate experimental and computational approaches to address scientific questions about these fundamental life processes,” Chan said, adding that she considers herself as a protein engineer studying the role of protein sequence and stability.

Chan is completing her graduate studies with both C. Robert Matthews, PhD, chair and professor of biochemistry & molecular pharmacology, and Konstantin B. Zeldovich, PhD, assistant professor of biochemistry & molecular pharmacology. Her research is focused on how proteins fold and maintain their three-dimensional structure.

“It’s the final step in central dogma of molecular biology, which relates DNA to RNA to functional protein. For many enzymes, the functional conformation is the native state. Stabilizing interactions determined by the sequence maintain this conformation for functionality and core function. It’s essential for daily life,” she said.

Her studies of the complexity of protein sequence, structure and stability, specifically in TIM barrel proteins, a highly represented fold in nature, lead to a recent publication of a paper, on which she is first author, in the journal Nature Communications.

Working with colleagues in the Matthews and Zeldovich labs, and adapting an assay from the lab of Daniel Bolon, PhD, professor of biochemistry & molecular pharmacology, Chan studied the relationship between the sequence of a protein, its structure and its fitness in supporting the growth of a yeast host.

She compared three orthologous TIM barrel proteins and showed that both sequence and structure constrain the fitness landscape during evolution. She found that mutations far from the active site of the protein can increase its catalytic power.

She credited her colleagues and primary investigators, and the collaborative environment at UMMS, in her ability to complete her research.

“The sense of community is very special at UMass,” Chan said. “Now, probably more than ever, biomedical research requires integration of multiple fields of science. Working here has provided me with a great opportunity to do so.”

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