| People
- Faculty
- Professor:
Thomas C. Bruice |
| Field(s): |
Bioorganic Chemistry |
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| Email: |
tcbruice@chem.ucsb.edu |
| Phone: |
(805)
893-
2044 |
Fax:
(805)
893-
4120 |
| Office: |
Bldg. 372 |
 |
Selected
Publications |
|
Go
to Research Group website |
| Bio: |
Dr. Bruice (Ph.D., 1954) served on the faculties of Yale,
Johns Hopkins and Cornell prior to coming to UCSB in 1964.
He has been a Guggenheim Fellow and is a member of the
National Academy of Sciences, American Academy of Arts
and Sciences and a fellow of the Royal Society of Chemistry.
He has received the major awards of the American Chemical
Society in the sub-disciplines of Bioorganic and Bioinorganic
chemistries, physical organic chemistry and biochemistry. |
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Current
Research
Our present research interests are in two areas: (i) nucleoside material chemistry (synthesis, characterization of interactions); and (ii) computational chemistry related to the mechanisms of enzyme catalysis (utilizing the programs AMBER, CHARMM, GAUSSIAN ETC.) Ongoing nucleoside problems involve the design, synthesis and study of compounds that may be used as antisence/antigene agents as well as research tools in the study of DNA-protein interactions. These materials consist of oligomers that are similar to DNA and are intended to bind to specific sites of the DNA or RNA in the target cell (examples DNG, RNG and DNmt) or agents that can bind into both the minor and major grooves of DNA (microgonotropens) to block the formation protein-DNA complexes (DNA-transcription factor).
Our computational chemistry work is based on known high resolution
x-ray coordinates of enzyme and enzyme complexes. These are
studied by molecular dynamic simulations and quantum chemical
calculations. We determine the structures of ground state reactive
enzyme·conformers and enzyme·transition states and the energies
separating these species. Examples of questions we ask are:
is Pauling’s precept correct that enzymes owe their catalytic
prowess to the tighter binding of the transition state as compared
to ground state & the means by which enzymes fashion ground
state conformations.
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| Selected
Research Publications |
| Luo, J, Author Luo Jia Luo, Jia , Bruice, TC, et al. Low-frequency normal modes in horse liver alcohol dehydrogenase and motions of residues involved in the enzymatic reaction BIOPHYS CHEM 126 (1-3): 80-85 MAR 2007. |
| Zhang, XH, Author Zhang Xiaohua Zhang, Xiaohua , Bruice, TC, et al. Diels-Alder ribozyme catalysis: A computational approach J AM CHEM SOC 129 (4): 1001-1007 JAN 31 2007. |
| Zhang, XH, Author Zhang Xiaohua Zhang, Xiaohua , Bruice, TC, et al. Temperature-dependent structure of the E center dot S complex of Bacillus stearothermophilus alcohol dehydrogenase BIOCHEMISTRY-US 46 (3): 837-843 JAN 23 2007. |
| Kahane, Alexandra L., Bruice, Thomas C. DNA sequence recognition in the minor groove by hairpin microgonotropens Bioorganic & Medicinal Chemistry Letters 16 (24): 6255-6261 DEC 15 2006. |
| Zhang, Xiaodong, Bruice, Thomas C.
Reaction mechanism of guanidinoacetate methyltransferase, concerted or step-wise
Proceedings of the National Academy of Sciences 103 (44): 16141-16146 OCT 31 2006. |
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