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Contact Information

Office: WEL 4.230C
Phone: 512-471-7859

David W. Hoffman

dhoffman@mail.utexas.edu

Associate Professor, Faculty
Graduate Advisor, Biochemistry, Graduate Studies



Research Group

Hoffman Lab



Education

MS, University of Massachusetts, 1982
BS, , 1979
PhD, Duke University, 1987



Affiliations

Institute for Cellular and Molecular Biology



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.

 



Representative Publications

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.