Also showcased during the Chemistry Carnival was the collaboration of Gokul with an artist in Puerto Rico to illustrate some of his science. Over the course of a few months, Gokul worked with Raisa Rodriguez Maldonado, from the University of Puerto Rico Mayagüez to bring to life his work with influenza viral infection. Her paintings highlight his study of the dynamics of hemagglutinin/receptor protein/protein interactions that permit cell entry, and ultimately, viral infection.
Science.Art.Wonder is sponsored by the Atlanta Science Festival and hopes to continue to be an integral interdisciplinary component of the annual festival.
On Friday, March 23, Emory’s Chemistry Department hosted the second annual “Chemistry Carnival” in conjunction with the Atlanta Science Festival. The event, which takes place in the Science Commons, Atrium, and courtyard fills the building with interactive demonstrations and games relevant to the research going on in the department. The Dyer lab participated with two different booths this year, Brooke and Monica at the “Electron Transfer Ring Toss” and Alexia at the “Laser Maze” in conjunction with Heaven Lab members.
The Electron Transfer Ring Toss demonstrates the basic principle of converting solar energy, where a photoexcited electron (or in this case, a glow bracelet taken from a big glittery sun) needs to be transferred somewhere else to successfully make electricity. Unfortunately, that transfer process is riddled with pitfalls, and is only about 20% efficient for most commercially available solar panels- most game participants scored even less than that when trying to ring the glowing Erlenmeyer flasks!
The Laser Maze used a safe red laser beam and several moveable mirrors to demonstrate the basics of manipulating light for experiments, relevant to so much of the research we do as a biophysical chemistry lab. Participants got firsthand experience with trying to control light through the maze, and witnessed some of the challenges of optical processes.
Check out more photos from the event! And a big thanks to Helen for taking some great pictures 🙂
Last week Brooke and Helen attended the first regional ComSciCon held in the southeast, ComSciConATL. ComSciCon is a science communication workshop designed to help graduate students find unique ways to interact with the general public and more effectively communicate their science. During the two day workshop at Georgia Tech, students had the chance to interact with local STEM PhD faculty and invited speakers, learn to incorporate storytelling and humor into their science narratives, network with local science writers and activists, and even sample some cutting-edge data visualization methods. Other benefits included mock interviews, professional editing of writing samples, and a keynote speech by Joe Hanson of PBS’s “It’s Okay to be Smart.”
An important theme of the conference was the use of personal stories to help humanize scientists and reach out across a diversity of audiences. Interdisciplinary collaboration and the use of multimedia and social media were all discussed as tools to not only underscore the importance of evidence-based research but also create an accessible conversation with the general public.
Last week’s JACS highlighted Morgan’s recent paper, “Activity-Related Microsecond Dynamics Revealed by Temperature-Jump Förster Resonance Energy Transfer Measurements on Thermophilic Alcohol Dehydrogenase.” The Spotlight summary, included below, underscores the uniqueness of the timescales we access in our lab and the overall importance of understanding enzyme dynamics in catalysis. Congrats on an outstanding paper, Morgan!
Making Sense of Protein Motion in Enzymes, Erika Gebel Berg (Ph.D.)
In recent years, scientists have come to appreciate that orchestrated protein motions are key drivers of enzyme activity. However, the details can be difficult to work out due to experimental limitations. Protein dynamics occur on multiple time scales, ranging from picoseconds to milliseconds, so measurement techniques must be carefully selected to probe the time scale of interest. Thomas Spiro, R. Brian Dyer, Judith Klinman, and colleagues use time-resolved temperature-jump FRET spectroscopy to probe the dynamics of thermophilic alcohol dehydrogenase, an enzyme model of the link between protein motion and activity (DOI: 10.1021/jacs.7b12369).
Previous researches in the Klinman Lab had indicated that protein motions facilitate the enzyme’s activity at temperature above 30 °C, but the timing and position of the motions was unknown. Now, by monitoring the energy transfer between NADH, the enzyme cofactor, and a nearby tryptophan side chain, the researchers observe a fast motion involving the enzyme active site that turns on above 30 °C. The fast relaxation rate is not detected at lower temperatures where the enzyme activity is compromised. This result implicates a link between thermally equilibrated, microsecond protein motions and the creation of active site configurations that facilitate catalysis. The work is a major step forward in understanding the functional role of enzyme dynamics.
Last week, Dr. Dyer visited the NIH in Bethesda, Maryland, at the invitation of Protein Conformation and Dynamics senior investigator Jennifer Lee. During the visit, Dyer gave a talk entitled “Membrane Protein Dynamics,” which was preceded by a poetic introduction that summarizes the research performed in our lab: