What is your educational background?
- Ph.D., Texas A&M University
- B.S., Grove City College
What are the main focuses of your research?
Proteins are synthesized by ribosomes as a linear sequence of amino acids. The sequence of amino acids in a protein is reflective of the gene sequence that codes for the protein. Beyond the genetic information, the primary structure holds all the information necessary for a protein to fold into an intricate, three-dimensional structure. This three-dimensional structure is the active, functional protein structure. It is also the structure of lowest free energy in the proteins normal environment. Unlike the genetic code, the "rules" for protein folding are not fully understood.
I am interested in determining the magnitude of the molecular forces that favor the folded protein over the unfolded protein. The basic approach is to measure thermodynamic parameters for protein unfolding in order to measure the values of the molecular forces. My protein thermodynamic data are available in the ProTherm Database. I am also interested in the application of this knowledge to increase the folding energy of medically or industrially important proteins.
Additionally, I am interested in developing and using computational algorithms for protein design.
What specific courses or specialties do you teach?
I teach Biochemistry I, Biochemistry II, and Biochemistry Seminar.
What is the most important piece of advice you give students to help them succeed?
I always encourage students to tackle new problems, not to be afraid to continue learning throughout life, and to be open to variety of possibilities. There will be change, of many more varieties than your area of interest, during your lifetime - be prepared to embrace that change. You will learn throughout your life - the exams will move from three or four a semester to every day. Accept it. Embrace it.