In my laboratory, a variety of biophysical methods are used to address important details of protein structure and its relevance for protein function and disease. Primary tools are X-ray crystallography and computer modeling, but these are combined with molecular biology tools of phage display and site-directed mutagenesis to confirm the models. I endeavor to engage each student in protein preparation or other "wet" lab experience, crystal growth, data collection and refinement, and computer modeling. The graduate career should provide enough hands on experience to build confidence that the student can draw on in his or her scientific career.
The main systems of interest at present are a small plant seed protein crambin and the structure/function of G protein coupled receptors. Crambin has provided a window into protein structure at the highest resolution ever seen for a protein - 0.67 Å - shorter than the C-H bond of 1Å. Discrete conformations of disordered side chains can be modeled as waving in concert on the protein surface.
G protein coupled receptors are transmembrane proteins that pass signals. Many are linked to diseases such as retinitis pigmentosa and schizophrenia. Our predicted structure of the D2 dopamine receptor showed that agonists can bind differently from antagonists. Semi-rigid drugs provide a good probe and test of our model. Drug design to target certain subtypes of receptors is planned.
Complete list by topic and most recent/significant.
Undergraduates, graduates, and postdoctoral students working in the lab.
Group meetings, etc.
Software developed in the lab and other software related to protein science.
Links of interest to protein and biochemistry sites.
"Crambin is a small plant seed protein. It has provided a window into protein structure at the highest resolution ever seen for a protein - 0.67 Å - shorter than the C-H bond of 1Å. Discrete conformations of disordered side chains can be modeled as waving in concert on the protein surface."
--Martha M. Teeter
This page has been accessed times since March 21, 1997. Research on crambin has been supported since 1981 by the National Science Foundation. This material is based upon work supported by the National Science Foundation under Grants No. PCM 8003929, PCM 8303024, DMB 8904337, and MCB 9219857
Any opinions, findings and conclusions or recomendations expressed in this material are those of the author(s) and do not necessarily reflect the views of the National Science Foundation (NSF).
Developed by M.M. Teeter and J.W. Bizzaro.