ASU's Hugh Downs School names Sarah J. Tracy interim director

June 30, 2021

The Hugh Downs School of Human Communication at Arizona State University has named Sarah J. Tracy as interim director beginning July 1.

Tracy replaces Paul Mongeau, a professor of interpersonal communication who served the school as interim director for the 2020–2021 academic year. The work of Sarah J. Tracy, who has taught and researched at ASU for 21 years, is focused on cultivating human flourishing, wisdom and connection at work. Download Full Image

In her new appointment as interim director, Tracy will continue the school’s leadership of research and pedagogy related to human communication in relationships, workplaces, communities and society.

A professor of organizational communication and qualitative methodology, Tracy (PhD 2000, University of Colorado) has taught and researched at ASU for 21 years. Her work is focused on cultivating human flourishing, wisdom and connection at work. She is the recipient of multiple scholarly honors, including the Distinguished Scholar Award from the National Communication Association (NCA) in 2020, the association’s highest accolade honoring a lifetime of scholarly achievement in human communication, as well as the Western States Communication Association’s Distinguished Teacher Award in 2019. 

“As an outstanding professor and award-winning researcher in the field of communication, I am confident Sarah will provide the innovative leadership needed as the Hugh Downs School of Human Communication’s new interim director,” said Pardis Mahdavi, dean of social sciences in The College of Liberal Arts and Sciences.

“I commend Paul Mongeau for his service as interim director and am grateful for his tremendous leadership during a challenging year.”

In returning to his faculty role, Mongeau will investigate the role of artificial intelligence in the persuasion process. He will also continue his long-standing research interest in the variety of “friends with benefits” relationships. 

Tracy’s research — which includes ethnographies on cruise ships, 911 call centers, correctional facilities and detailed case analyses of burnout, bullying, leadership and compassion — is regularly featured in courses and books related to organizational communication and qualitative research methods. Her scholarship has extended knowledge about organizational leadership, workplace well-being, conversation, identity and emotion. This research has garnered a number of top articles, papers and disciplinary awards, including the prestigious Charles Woolbert Award from the NCA.

Tracy co-founded the Transformation Project, a consortium of faculty, students and community members who seek to discover and promote creative change processes that encourage healthy communication patterns, collaborative group behavior and equitable forms of social organization.

Hugh Downs School Assistant Professor Elissa Adame has collaborated with Tracy through the Transformation Project and through developing, practicing and testing a transformational leadership approach.

Book Cover

NCA’s Organizational Communication Division’s 2020
Outstanding Textbook of the Year Award went to
Professor Sarah J. Tracy's "Qualitative Research Methods."

“I have seen through our work together how Sarah is dedicated to leading in a way that will create a future that meets the needs and concerns of a range of stakeholders," said Adame. "Not only does Sarah study transformational leadership, she lives it, and she gives others the courage and resources to do the same.”

Tracy has several key goals as she moves into the interim director role.

“Given the disruptions of the pandemic, I hope to provide a platform for meaningful connection, recreation and growth among faculty and students while also building the school’s momentum of innovative research, dedication to justice and equity, and historical excellence in incisive and inclusive pedagogy,” she said.

She has taught a mix of over 20 courses and advised more than 45 graduate students at ASU. Her most recent book, “Qualitative Research Methods: Collecting Evidence, Crafting Analysis, Communication Impact” received NCA’s Organizational Communication Division’s 2020 Outstanding Textbook of the Year Award.

One of Tracy’s favorite adages in terms of work and play is: “Anything worth doing well is worth doing badly in the beginning.” She is currently keeping busy outside of work by “doing badly” as she gets back into playing the piano. Additionally, she provides interdisciplinary and public outreach workshops, mentors through Big Brothers/Big Sisters, contributes to her “Possibility Detective” blog and hosts a YouTube channel called “Get Your Qual On.” 

Manager, Marketing and Communication, Hugh Downs School of Human Communication


Hope for more effective antibiotics comes from ASU research of protein structure, folding and dynamics

June 30, 2021

Enzymes are one of the most important biological compounds because they make life possible by increasing the speed of reactions inside and outside cells. In cells, enzymes carry out functions such as protein synthesis, DNA replication and energy production.

To do these and other activities, enzymes are both complex and specific. For example, lactase is the enzyme that breaks down lactose, a sugar found in milk, into simpler sugars, glucose and galactose. However, the enzyme lactase will not break down the sugar maltose; the enzyme maltase does that. Enzyme evolution resulting in antibiotic specificity and increased resistance. Download Full Image

The specificity and complexity of enzymes makes them difficult for researchers to study or design enzymes for new applications. Arizona State University researchers Tushar Modi and Banu Ozkan of the Department of Physics, and Wade Van Horn and Mubark Mebrat, both of the School of Molecular Sciences, along with colleagues from other institutions, report on a breakthrough that improves understanding of the relationship between protein structure, dynamics and function. Their results have important implications for medical, biotechnological and molecular research.

Their article, "Hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity," published in Nature Communications, focuses on the structure and function of beta-lactamase, a protein enzyme in bacteria that breaks down the structure of beta-lactam antibiotics, such as penicillin and amoxicillin, that are used to treat bacterial infections.

In their quest to understand how bacteria develop antibiotic resistance, these scientists determined that rather than requiring a separate gene to code for each enzyme, mutations — which result in changes as minor as one amino acid in the protein structure — can shift the location of a hinge where the protein moves (i.e., dynamics), allowing it to better fit an existing molecule, or even interact with a completely new molecule.

Rather than protein structure being fixed, as was thought in the past, researchers are discovering that protein structure and shape is dynamic within a class of proteins.

“This study provides evidence that the conformational dynamics of a protein is modulated, if not determined, not by the general structure but by the combination of its flexible and rigid regions,” School of Molecular Sciences graduate student Mebrat notes. “This suggests that over an evolutionary timeline, proteins may retain their general structures and by adjusting flexible and rigid regions can modulate function. In the case of beta-lactamase, bacterial organisms can reemploy the same enzyme to degrade different antibiotics or degrade with greater specificity and efficiency.”

A dynamics-based approach to unraveling protein evolution and function can also be applied to engineering proteins that are more effective.

“Enzyme design is the most difficult task in protein design," Ozkan said. "Indeed, the majority of designed enzymes are significantly less efficient than natural enzymes.”

“Our dynamics-based approach, however, allows us to devise design principles to engineer specialized modern proteins," said Modi.

These designed enzymes can be employed to degrade plastics or fight infections, among other things. Additionally, understanding how antibiotics are degraded can help molecular scientists engineer antibiotics that are less susceptible to bacterial resistance in the future.

“A major problem that has arisen over the last century is antibiotic-resistant bacteria,” Van Horn said. “This study offers insights into an enzyme that degrades antibiotics, which is important for the development of new and more effective drugs.”

James Klemaszewski

Science writer, School of Molecular Sciences