Contact InformationOffice: WEL 4.230C
David W. Hoffmandhoffman@mail.utexas.edu
Associate Professor, Faculty
Graduate Advisor, Biochemistry, Graduate Studies
MS, University of Massachusetts, 1982
BS, , 1979
PhD, Duke University, 1987
Protein and nucleic acid structure; NMR spectroscopy
Ongoing research projects are related to protein and RNA structure and dynamics, and RNA-protein interactions, with an emphasis on components of the protein synthesis apparatus. Nuclear magnetic resonance (NMR) spectroscopy is extensively used in our investigations.
Structural analysis of components of the translation initiation complex
The process by which the ribosome, tRNAs, initiation factors and elongation factors work together to synthesize a protein is of central importance within all forms of life. A detailed knowledge of the structure and interactions of these components will surely be required as part of a complete understanding of translation, and in particular, how the initiator tRNA and ribosome are brought together to initiate translation at the correct codon. Toward this goal, we have recently expressed and purified several of the most conserved components of the initiation complex, and analyses using multi-dimensional NMR and x-ray methods are underway.
Structural analysis of the RNase P complex
RNase P is a multi-component RNA-protein complex that cleaves the 5' termini of precursor tRNA in an essential step toward the synthesis of mature tRNA. The structure of RNase P is being determined using a combination of NMR and x-ray crystallographic methods, where the RNase P of Archaeoglobus fulgidus is being used as a model system.
Chu, Y., Hoffman, D.W. & Iverson, B.L. "A pseudocatenane structure formed between DNA and a cyclic bisintercalator" J. Amer. Chem. Soc. 131 (2009): 3499-3508.
Tao, Zhihua, Gao, P., Hoffman, D.W. & Liu, H.w. "Domain C of human poly-(ADP-ribose) polymerase-1 is important for enzyme activity and contains a novel zinc-ribbon motif" Biochemistry 47 (2008): 5804-5813.
Montemayor, E.J. & Hoffman, D.W. "Crystal structure of spermidine/spermine N1-acetyltransferase in complex with spermine provides insights into substrate binding and catalysis" Biochemistry 47 (2008): 9145-9153.
Monzingo, A.F., Dhaliwal, S., Dutt-Chadhuri, A., Lyon, A., Sadow, J.H., Hoffman, D.W., Robertus, J.D. & Browning, K.S. "The structure of translation initiation factor eIF4E from wheat reveals a novel disulfide bond" Plant Physiol. 143 (2007): 1504-1518.