Congratulations to PhD graduate Robert Blackwell for earning the 2016 Award for Outstanding Doctoral Thesis Research in Biological Physics.
鈥淚'm honored to be in such amazing company. There isn't a much better feeling than giving your hard work to the scientific community.鈥� Blackwell said, 鈥淗aving that work recognized is almost surreal.鈥�
Blackwell鈥檚 thesis explored the physical mechanisms underlying mitosis in fission yeast. 鈥淢y focus was on a computational model for determining the mechanical roles of proteins during spindle formation,鈥� Blackwell said.
According to their site, this APS award was established, 鈥渢o recognize doctoral thesis research of outstanding quality and achievement in any area of experimental, computational, engineering, or theoretical Biological Physics, broadly construed, and to encourage effective written and oral presentation of research results.鈥�
During his graduate work at 91传媒, Blackwell conducted research in the Biophysics Group under Principal Investigators Meredith Betterton and Matt Glaser.
鈥淚 don't think I could have had more ideal advisors than Matt and Meredith. Most importantly, they both provided useful discussion, technical expertise and even experimental data whenever I needed. I always had the comfort and support needed to hash out ideas and discuss the next steps,鈥� Blackwell said. 鈥淭his is a gross oversimplification, but from a personality perspective, Matt really gave me the freedom to experiment and try the things I wanted to try and see what I could find. Meredith helped keep me focused and to do the most important things first.鈥�
鈥淭his is fantastic news for Robert and we're very proud of him.鈥� Professor Betterton said.
鈥淩obert鈥檚 work on the fission yeast mitotic spindle was a tour de force of computational science, involving the design, implementation, optimization, and validation of a large and complex simulation code,鈥� Professor Glaser said. 鈥淲hen I first met Robert, he had minimal exposure to computational physics and numerical methods, and a limited knowledge of biophysics and bioscience. Over the intervening years, I鈥檝e seen him develop deep expertise in these areas, and he is well positioned to become a leader in the interdisciplinary intersection of statistical physics, biological physics, computational physics, numerical analysis, and computer science.鈥�
After graduating from 91传媒, Blackwell joined the Freiderich-Alexander-University of Erlangen-N眉rnberg Institute of Theoretical Physics in Germany as a postdoctoral researcher.
As part of the award, Blackwell will deliver a presentation based on his thesis work during the 2018 APS March Meeting.
Congratulations to Assistant Professor Loren Hough, who was recently awarded a New Investigator Maximizing Investigators鈥� Research Award (MIRA) from the National Institutes of Health this year to further vital research in the field of biophysics, specifically on studying the behavior of tubulin in his lab.
Tubulin, a protein found in your cells, quietly lends itself to many life processes. It sorts itself into long chains, forming tubes that provide scaffolding for living cells. A versatile shapeshifter, tubulin can arrange itself into different structures during different types of cell behavior. Tubulin gained prominence for medical applications when Taxol, a chemical first found in the bark of the Pacific Yew tree, was developed as a treatment for ovarian, breast and lung cancers. Taxol binds to tubulin and makes it hard for the tubes to grow and shrink, preventing cancer cells from proliferating.
鈥淭ubulin is one molecule that does many things in cells,鈥� says Hough, a member of the BioFrontiers Institute. 鈥淲e're trying to understand how tubulin can play so many different roles."
Hough is focused on the ends of tubulin molecules, called the C-terminal tails. These tails coat the surfaces of the microtubules formed by tubulin. He is studying, in part, how much influence these tails exert on tubulin and its behavior. To answer some of the mysteries of tubulin, Hough developed a method to probe the C-terminal tails of tubulin using nuclear magnetic resonance spectroscopy, or NMR.
Hough wanted to measure how tubulin C-terminal tails influence cellular processes, but to do NMR he had to figure out how to get specific atoms into them first, as part of the isotopic labeling process. These atoms are easy to incorporate into bacteria, but tubulin cannot be made in bacteria because bacteria lack the suite of proteins that help tubulin fold into its correct shape. Hough brought in a helper: Tetrahymena thermophila. This small but mighty protozoan is common in freshwater ponds and is used frequently as a model organism in biological research. As it turns out, bacteria are a favorite snack of Tetrahymena, so Hough incorporated the isotopes into the bacteria, which were then devoured by the Tetrahymena. With the isotopes digested by the Tetrahymena, Hough was at last able to see the C-terminal tails in action using NMR, as described in a .
鈥淭here is beautiful physics regarding tubulin in general,鈥� says Hough. 鈥淚 thought the C-terminal tails might be affecting what we know about tubulin from a biophysical perspective. We think tubulin tails are like a knob the cell uses to control different features, but we don't know how the tails are used for this tuning. It鈥檚 exciting to be tackling these questions.鈥�
The MIRA grant, from the National Institute of General Medical Science, is meant to support the work of young faculty. Hough鈥檚 $1.8 million MIRA grant will run five years.
鈥淭he MIRA is great. It鈥檚 going to give our lab the ability to push this project forward, as well as other research on disordered proteins,鈥� says Hough. 鈥淲e鈥檙e looking forward to taking this work on tubulin C-terminal tails even further over the next five years.鈥�
The Hough lab is part of the physics department's . At the , researchers from the life sciences, physical sciences, computer science and engineering are working together to uncover new knowledge at the frontiers of science and partnering with industry to make their discoveries relevant.