Molecular dynamics simulations suggest a structural basis for the slow-onset inhibition of KasA by thiolactomycin and provide insights for TB drug discovery
By Brian Miranda
Before I entered high school, my older brother returned from his lab each day with a story about his work. I could always hear his excitement when he talked about his project. I knew I wanted to try my hand at research but the microarray analysis procedures he described did not appeal to me. Volunteering then at a local hospital, I wanted to pursue a hands-on study of disease, but was unsure how to go about it. When I made the decision in the spring of 2008 to do summer research, I consulted one of my teachers; he recommended Dr. Carlos Simmerling’s lab, which specialized in computational structural biology at Stony Brook University. And in my first visit to the Simmerling Lab, I was fascinated by the work of two graduate students who were visualizing proteins folding on the computer. The computer offered such a controlled environment for studying biological systems. Working mostly with software tutorials my first summer there, I also found that any experiment required my input at every step it was rewarding to have complete control. I soon began my own analysis of an enzyme in the tuberculosis (TB) pathogen. The freedom I had to study the complexities of TB under such controlled conditions inspired me to continue my project for the next three years.