Scholars 2005

2005 Future - Materials Science

French Timothy

Personal Details:
Department of Chemistry - Yale University, USA

Title of Research: 
"Investigation of Librational Coupling in Crystalline L-Alanine Using Two-Dimensional Terahertz Spectroscopy "

Updates

January 2017

I was awarded the Dan David Prize in 2005 for the Future Track in Materials Science while I was a graduate student in Prof. Charles Schmuttenmaer's lab at Yale University.  After graduating with my PhD in chemistry from Yale in 2007, I was a non-tenure track faculty member at Harvard University teaching physics and physical chemistry from 2008-2012.  From there I moved to Chicago, IL, USA, to DePaul University where I was a non-tenure-track faculty member from 2012-2014.  Starting in 2014 I moved to the tenure track at DePaul in the position of Assistant Professor.  My research group performs chemistry and physics education research.  One major thread through my research and teaching is the interdisciplinary nature of the sciences.  I've been interviewed a few times for some of DePaul's internal and alumni publications about a new class that I created with a colleague in the writing department here on campus

http://csh.depaul.edu/faculty-staff/faculty-a-z/Pages/chemistry/timothy-french.aspx

http://www.depaulnewsline.com/features/write-stuff-new-science-course-helps-chemists-communicate

 

January 2006

My research uses terahertz (far-infrared) spectroscopy to study molecular motions in solid-state amino acids. Intermolecular motions have signatures in this energy regime. Presently, we are looking at the various enantiomers (D, L, and DL) of tryptophan. We've seen that peaks in the terahertz spectrum are dependent upon enantiomer. In the case of tryptophan, L and its mirror image D show peaks, whereas a 50-50 mixture of D and L (appropriately known as DL) does not. Since we're probing such low energies, these data imply that their crystal structures are different. By studying how intermolecular motions and crystal configurations manifest themselves in the terahertz regime we hope to have a better handle of how more complex motions act (eg. coupled motions found in numerous biomolecules, which may have a hand in protein folding).

In the past few months, I have been focused mainly on the theoretical/computational aspect of this project. The xray structure is completely solved for DL Tryptophan, whereas only the space group (ie symmetry) of the other two are known. Using the well-known molecular mechanics program CHARMM, I hope to determine the structures of crystalline L and D Tryptophan that are consistent with the spectra we have collected. So far, I am trying to reproduce the known values for DL Tryptophan. Very recently, in fact, I have been able to reproduce qualitatively the low-energy DL spectrum. This bolsters our faith in the reliability of the computational methods used and their ability to predict structures that are not fully known. We plan on publishing this research in the months to come.

I am midway through my fourth year of the PhD program in chemistry at Yale University. I hope to attain my PhD during the 2007-2008 academic year, after which I will apply for a Science and Public Policy Fellowship offered by the US government. These fellowships are put in place for PhD scientists to work in the public sector for a year in order to get a better feel for the interplay between these two realms. One that sparks my interest is in "threat reduction", specifically the bookkeeping/collection of WMDs and loose nukes in the former USSR. If I enjoy this line of work, I will look for a permanent position in government; if not, I will most likely join the faculty of a college and focus on teaching and science education research.

I am extremely grateful for being awarded a 2005 Dan David Prize Scholarship recognizing the research that I do.