Faculty (Go To Lecturers)
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Aragon, Sergio B.A. (1971) Rice Univ. ,Physics Ph.D. (1976) Stanford University, Physical Chemistry At SFSU since 1985 Tel: 415.338.7712 e-mail: aragons@sfsu.edu Web Site: Sergio Aragon |
Research Area: Physical Chemistry
Study of macromolecules (natural or synthetic) in solution by dynamic laser light scattering, transient electric birefringence and Monte Carlo simulation techniques. Measurements are made of various transport properties of systems at or near equilibrium to obtain information on size, conformation, shape and flexibility. In addition, a major thrust of this research is to develop appropriate theoretical models relevant to the measurements mentioned above. The theory involves the statistical mechanics
Of molecular motion in fluids, including internal motions, and the electromagnetics of scattering processes in the Rayleigh-Debye and Mie regimes. Computer algebra techniques are used in the theoretical and computational aspects of these problems. Recent research includes the application of boundary element methods for the accurate hydrodynamic computation of transport properties of proteins and nucleic acids in solution with the stick boundary condition and small to intermediate size molecules with the slip boundary condition.
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Teaster Baird BS (1992) Tougaloo College, Chemistry Ph.D. (1997) Duke University, Biochemistry At SFSU since 2002 Tel: 415.405.0935, Thornton Hall, room 817B e-mail: tbaird@sfsu.edu |
Research Area: Biochemistry
My research interests revolve around understanding the relationship between the structures of certain proteins, namely metallo-enzymes and proteases, and their functions. Our understanding of how the three dimensional structure of a protein dictates its function is limited. However, by examining known protein structures and making both semi-random and logical changes in the structure of a protein, we can rationalize how certain structural features give rise to certain aspects of its function. In some cases, this understanding can allow one to predictably introduce new functionalities into existing protein scaffolds. Experiments in my laboratory will be focused on designing and introducing metal binding sites into serine proteases to investigate their mechanisms of activation, altering serine protease structure to introduce new catalytic machinery, and examining catalytic and structural zinc binding sites in zinc metallo-proteins to dissect the factors that determine how the metal is used. Techniques used to design, produce and characterize the engineered proteins will include site-directed and random mutagenesis, computer modeling, the incorporation of non-natural amino acids and UV-Vis and fluorescence spectroscopy.
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Berkman, Cliff B.A. (1986) Lake Forest College, Chemistry Ph.D. Loyola University of Chicago, 1993 At SFSU since 1996 Tel: 415.338.6495 e-mail: cberkman@sfsu.edu Web Site: http://userwww.sfsu.edu/~cberkman |
Research Area: Organic Chemistry
Synthesis, resolution, and biochemical evaluation of chiral phosphorus-containing inhibitors of metallopeptidases related to cancer, folate processing, and neurodegenerative diseases.
The research in my laboratory is primarily concerned with design of novel enzymes inhibitors for the use in sensitizing tumor cells to common chemotherapeutic strategies. Specifically, we are interested in phosphorus- and sulfur-containing transition-state analogs inhibitors of these target enzymes. To this end, we focus also on the preparation of conformationally restricted substrates for such enzymes in order to probe their structural requirements and to ultimately design analogous inhibitors with enhanced selectivity.
We are also interested in the design and synthesis of conformationally constrained molecules for use as pro-prodrugs. Such molecules require a primary bioactivation step which is followed by a rapid intramolecular release of a drug. Consequently, these compounds may allow for the specific or timed release of potent drugs at a desired site of action.
Finally, we are beginning to design and develop novel synthetic alternatives to the organophosphorus insecticide Malathion. Such compounds will be designed to be insensitive to the secondary problems associated with acute poisoning by impurities found in commercial Malathion formulations. Utilizing our current understanding of the mechanism by which these impurities act to inhibit target enzymes, we will construct synthetic analogs that both confirm this mechanism and circumvent it.
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Buttlaire, Daniel H. B.A. (1963) University of Denver, Chemistry Ph.D. (1970) University of Kansas, Biochemistry Professor of Chemistry and Biochemistry, SFSU Dean of Undergraduate Studies, SFSU At SFSU since 1975 Tel: 415.338.1288 e-mail: db@sfsu.edu Web Site: http://ariel.sfsu.edu/adm/db/info/hp.htm |
Research Area: Biochemistry
Physical biochemistry/molecular biophysics. Structure-function relationships in macromolecular systems.
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DeWitt, Jane D. B. S. (1986) Univ. of CA Santa Barbara, Chemistry Ph. D. (1992) Stanford University, Chemistry At SFSU since 1995 Tel: 415.338.1895 email: dewitt@sfsu.edu |
Research Area: Bioinorganic and Environmental Chemistry
The research in my laboratory focuses on understanding the mechanisms of heavy metal accumulation and transformation in higher plant systems from a chemical and molecular perspective. A variety of physical and biochemical techniques are being used to investigate the distribution and transformation of heavy metals by plants including atomic absorption spectroscopy, mass spectrometry, HPLC, size exclusion chromatography and X ray absorption spectroscopy. The goals of this research are to determine the change in speciation (oxidation state, geometry, coordination environment) that occurs upon accumulation of the metals by plants and to identify the biomolecules involved in metal complexation, thus providing insight into mechanisms of heavy metal tolerance in plants. The effect of heavy metals on gene expression is being investigated using polymerase chain reaction fingerprinting techniques and subtractive hybridization techniques. We hope to identify the genes involved in the transformation pathways we are characterizing by the techniques described above.
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Erden, Ihsan B.S. (1971,Vordiplom) Georg-August Univ. Göttingen, Chemistry M.S. (1973,Diplom) Georg-August Univ. Göttingen, Chemistry Ph.D. (1977) Georg-August Univ. Göttingen, Chemistry At SFSU since 1981 Tel: 415.338.1627 email: ierden@sfsu.edu Web Site: http://userwww.sfsu.edu/~ierden/welcome.html |
Research Area: Organic Chemistry
Organic Synthesis, chemistry of singlet oxygen and organic peroxides, chemistry of fulvenes, small ring compounds, cycloadditions, heterocyclic chemistry. One of our ongoing projects focuses on the development of new synthetic methodologies based on functionalized allene oxides derived from saturated fulvene endoperoxides. Another project concerns the synthesis of nitrogen heterocycles based on a novel aza-Robinson annulation reaction. Among the target molecules are five-membered nitrogen heterocycles found in the naturally occurring family of tetramic acid antibiotics. Furthermore, environmentally benign oxidative C-C and C=N cleavage reactions are under investigation.
Research Area: Synthetic Organic Chemistry, Chemistry of Singlet Oxygen,
Organic peroxides, Oxygen and Nitrogen Heterocycles, Small Ring Compounds,
Current projects involve the synthesis of new synthetic methods based on organic peroxides. In particular, the chemistry of allene oxides derived from saturated fulvene
endoperoxides is being studied extensively.
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Esquerra, Raymond B.Sc. (1990) Stanford Univ., Physics Ph.D. (1997) Univ. CA, Santa Cruz, Chemistry At SFSU since 2000 Tel: 415.338.3444 email: esquerra@sfsu.edu |
My research investigates the nature of protein function and the molecular basis of disease using a variety of biochemical and biophysical tools. I use specialized time-resolved absorption spectroscopy to determine the kinetics of protein function. In addition to kinetic investigations of normal protein function, I would like to determine how nonenzymatic glycosylation compromises protein function, providing a better understanding of how it contributes to disease (as in the case of diabetes), and how chemical modification, in general, affects protein function. The tools that my research uses are applicable to many biomolecules, allowing for a better understanding of how proteins perform their miraculous chemistries.
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Gassner, George B.S. (1989) Univ. of Minnesota, Biochemistry Ph.D (1995) Univ. of Michigan, Biochemistry At SFSU since 2000 Tel: 415. 338.1366 email: gassner@sfsu.edu |
Reasearch Area: Biochemistry
We are interested in studying enzymes which employ transition metals and orgainic cofactors in their reaction mechanisms. This interesting group of biocatalysts has functions both in microbial metabolism and in the metabolic pathways, organogenesis, and homeostasis of higher organisms. Our studies will include oxidases and hydroxylases involved in microbial oxidation of organic and halogenated organic compounds such and polychlorinated biphenyls (PCB's), amino acid hydroxylases, which produce reactive groups that cross-link connective tissues, diamine oxidase, a DNA binding enzyme which transforms biological amines to aldehydes, and enzymes
in the pathway of heme catabolism, including heme oxygenase and biliverdin reductase.
Biophysical studies will include: (1) Investigation of individual steps in enzyme reaction mechanisms by continuous flow, stopped-flow, and rapid-quench experiments monitoring changes in surface plasmon resonance, fluorescence, absorbance, and other spectroscopic signals. (2) Thermodynamic measurements of small molecule-protein, DNA-protein, and protein-protein binding interactions by electrophoresis, titration calorimetry, analytical ultracentrifugation, and spectroscopic methods (3)
Measurement of electron-transfer rates and equilibrium midpoint potentials of redox enzymes. Biochemical studies will include protein purification, eukaryotic and prokaryotic cell culture, and recombinant DNA technologies applied to the isolation and expression of the enzyme systems of interest.
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Gerber, Nancy B.S. (1988) Univ. of Florida, Physics Ph.D. (1993) Univ. of Illinois, Champaign-Urbana, Biochemistry At SFSU since 1996 Tel: 415.338.1160 email: ngerber@sfsu.edu |
Research Area: Metalloprotein Biochemistry
The study of structure-function relationships in redox and metalloproteins with particular emphasis on heme proteins. Areas of study include enzyme mechanisms, electron transport, protein-protein interactions, and protein engineering for altered specificities/activities. Techniques used include side-directed and semi-random mutagenesis, UV/Vis, EPR and FTIR spectroscopies, and stopped-flow spectrophotometry as well as standard heterologous protein expression and purification techniques. Current areas of study are cytochrome P-450 enzymes and soluble guanylyl cyclase.
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Scott Gronert B. S., California State University at Long Beach, 1983 Ph. D., University of California at Berkeley, 1987 At SFSU since 1990 Tel: 415-338-7709 e-mail: sgronert@sfsu.edu Web Page: http://userwww.sfsu.edu/~sgronert |
Research Area: Organic Chemistry
The use of mass spectrometry to study reaction processes in organic and biochemical systems. Gas phase studies of organic reaction mechanisms such as substitution and elimination. Development of methods for sequencing and characterizing peptides via mass spectrometry. Application of computational approaches to the study of reaction mechanisms and gas phase binding interactions
Dr. Gronert’s research focuses on using mass spectrometry as a tool for studying the details of reactions in organic and biochemical systems. Recently, gas phase dianions have been used to assess the competition between substitution and elimination reactions. The work is leading to new insights into these important organic reactions. Another part of the research group works on the gas phase reactions of peptides. The goal is develop new approaches for efficiently sequencing peptides and proteins by mass spectrometry. These studies also provide information concerning the secondary structure of the peptides as well as the location of post-translational modifications. Finally, Dr. Gronert’s research group is investigating the reactions of gas phase salt complexes with an emphasis on chiral recognition. The work is presently funded by the National Science Foundation and the National Institutes of Health.
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Ichimura, Andrew S. Assistant Professor Tel: 415.405.0721 Fax: 415.338.2384 email: ichimura@sfsu.edu |
Research Area: Physical Chemistry/Materials Chemistry
Self-assembly of zeolite monolayers and multilayered materials; spectroscopic (FTIR, UV-vis-NIR, EPR, ENDOR) investigations of novel solid state reducing agents; computational chemistry. Our research focuses on the physical properties and applications of alkali metal doped pure silica zeolites. Zeolites are microporous materials that have traditionally found use in catalysis, separations, and exchange processes. However, zeolites with conducting or semiconducting properties might find use in the development of chemical or optical sensors and detectors. Our materials are prepared by addition of alkali metals (M=Na, K, Rb, Cs) to silica zeolites (SZ) to form a novel class of intercalation compounds, M@SZ. These systems are predicted to be metallic and therefore good conductors. They are also excellent reducing agents. Specifically, our research objectives are to (1) develop strategies to prepare thin films of these conductive zeolites on gold surfaces or ITO glass, and (2) to explore the potential of M@SZ as novel solid state reducing agents for organic and inorganic substrates. In principle, the size and shape selectivity intrinsic to zeolitic structures coupled with the intercalated alkali metal may yield reagents with chemistry quite different from what is observed in homogeneous solution.
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Keeffe, James R. B.A. (1959), Santa Barbara College, Chemistry Ph.D. (1964) Univ. of Washington, Organic Chemistry At SFSU since 1965 Tel: 415.338.1117 email: keeffe@sfsu.edu |
Research Area: Organic Chemistry
Physical organic chemistry, reaction mechanisms, structure-reactivity relationships among C-H acids, molecular modeling for undergraduate organic chemistry students.
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Mary Luckey B.A.(1970) Hope College, Chemistry Ph.D.(1976) Univ. of CA, Berkeley, Biochemistry At SFSU since 1982 Tel: 415-338-7714 e-mail: luckey@sfsu.edu web page: http://lewis.sfsu.edu/luckey/ |
Research Area: Biochemistry
Structure, function and biogenesis of LamB protein, the maltoporin in the outer membrane of Escherichia coli: Purification and reconstitution of LamB and mutant LamB proteins. Role of the disulfide bond in LamB protein in protein folding, trimer assembly and integration in the outer membrane. Role of chaperones in LamB protein biogenesis.
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Macher, Bruce A. B.S. (1971) Univ. of CA, Riverside, Biochemistry Ph.D. (1976) Univ. of CA, Riverside, Biochemistry At SFSU since 1987 Tel: 415.338.7091 e-mail: macher@sfsu.edu |
Research Area: Biochemistry
Structure/function studies of a family of enzymes (glycosyltransferases)
involved in the synthesis of carbohydrate structures involved in immune
response, rejection of transplanted tissues and development. Molecular
biology, protein chemistry, mass spectrometry and enzymological studies are
used in combination to determine which amino acids are responsible for the
fine substrate specificity of each enzyme, in binding substrates and
mediating the reactions catalyzed by these proteins.
Dr. Macher is the Associate Dean for Research and Sponsored Programs at
SFSU. He is also the Director of the Office for Biomedical Research and
administers the Research Infrastructure program funded by NIH for SFSU
which serves faculty involved in biomedical research from seven departments
on campus. His research has been funded by NIH and NSF for more than
twenty years and he has supervised and supported the research efforts of
many students, who are either currently enrolled in Ph.D. programs or
employed at various biotechnology companies in the Bay Area. Several MS
students are currently working in the laboratory on a range of projects
that include site directed mutagenesis, protein purification, mass
spectrometry and enzymology of glycosyltransferases.
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Manning, Bruce B.S. (1985) Univ.of Massachusetts, Environmental Science Ph.D. (1993) Univ. of CA Davis, Environmental Chemistry At SFSU since 1999 Tel: 415.338.1292 e-mail: bmanning@sfsu.edu |
Research Area: Environmental - Analytical
Determination of molecular surface structures of trace elements and oxyanions adsorbed on synthetic metal oxides, clay minerals, and soils using extended X-ray absorption fine structure spectroscopy (EXAFS). Separation and detection of redox sensitive elements (arsenic(III)/(V), selenium(IV)/(VI), and chromium(III)/(VI)) by hyphenated analytical techniques. Synthesis and characterization of metal oxides and metal oxide-coated substrates. Equilibrium and surface complexation chemical modeling of environmental systems.
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Orenberg, James B.A. (1965) Williams College, Chemistry Ph.D. (1969) The Pennsylvania State Univ. (Chemistry) At SFSU since 1972 Tel: 415.338.1288 e-mail: orenberg@sfsu.edu |
Research Area: Analytical Chemistry
Evaluation of Mars Soil Analog Materials by chemical and spectral (reflectance spectroscopy) means coupled with head space gas chromatography of simulations of the Viking Biology experiments in order to draw conclusions regarding the composition and structure of the Martian soil, its water content, and its relationship to the geochemistry, atmosphere volatile cycles, and possible primitive exobiological and organic processes of the planet.
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Palmer, Pete B.S. (1983) Canisius College, Chemistry Ph.D. (1988) , Michigan State Univ., Analytical Chemistry At SFSU since 1994 Tel: 415.338.7717 e-mail: palmer@sfsu.edu |
Research Area: Analytical-Environmental Chemistry
My research interests focus on the development, characterization, and application of mass spectrometric techniques for monitoring pollutants in the environment. This research involves the use of EPA-approved Gas Chromatography/Mass Spectrometry (GC/MS) methods and new Direct Sampling Mass Spectrometry (DSMS) techniques. The latter represents a new technology that promises to revolutionize the way air quality monitoring is performed. Relevant characteristics of DSMS include excellent sensitivity,
tunable selectivity, the ability to do real-time monitoring, and a small size which makes the technique amenable to field applications. Much of our efforts to date involve the development of improved sample introductionsystems to extend detection limits down to low part-per-trillion levels. Additional work involves the study of various ionization methods and mass spectrometry scan modes for selective detection of volatile organic
compounds (VOCs) in complex matrices. Some of our group's environmental applications to date include the analysis of VOCs in air samples from the Russian Space Station Mir, the measurement of regional and temporal variations in air pollutants in the San Francisco Bay Area, and the analysis of pesticide contaminants on Native American objects.
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Simonis, Ursula Diploma (1982) Westfalishce Wilhelms-Univ., Munster, Chemistry Ph.D. (1985) Westfalishce Wilhelms-Univ., Munster, Chemistry At SFSU since 1985 Tel: 415.338.1656 e-mail: uschi@sfsu.edu |
Research Area: Bioinorganic Chemistry
Investigations of biologically relevant paramagnetic iron porphyrin, chromium, zinc, and organocobalt complexes to mimic the active sites of important heme proteins, the glucose tolerance factor, zinc enzymes, and vitamin B12. Synthesis of new model complexes and solution structure analysis by spectroscopic methods, primarily by modern multi-dimensional NMR spectroscopy to obtain new insights into the structure-function relationships of the corresponding biomolecules. Investigations and structural characterization of small organic molecules, porphyrins and metalloporphyrins embedded in model membranes aimed at synthesizing clinically useful drugs for cancer detection and therapy. Development of the multi-dimensional NMR methodology for the resonance assignment and structural characterization of paramagnetic molecules to determine the scope and limits of multi-nuclear and multi-dimensional NMR spectroscopy for the structural analysis of paramagnetic molecules.
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Trautman, Raymond B.A. (1977) Trinity College, Univ. of Dublin, Chemistry Ph.D. (1980) Trinity College, Univ. of Dublin, Chemistry At SFSU since 1987 Tel: 415.338.2379 e-mail: trautman@sfsu.edu |
Research Area: Inorganic chemistry
Photochemistry and photophysics of organometallic compounds, especially metal alkyl and metal alkenyl compounds. Reaction mechanisms in solution related to homogeneous catalysis. Intercalation chemistry of zeolites, adsorption of heavy metals by zeolites and iron oxides.
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Wu, Weiming B.S. (1986) Nanjing Univ., Chemistry Ph.D. (1992) Univ. of Illinois, Chemistry At SFSU since 1995 Tel: 415.338.1436 e-mail: wuw@sfsu.edu |
Research Area: Bioorganic chemistry.
Our research group is interested in the design, synthesis, and study of enzyme substrate analogs. These analogs are designed to elucidate the catalytic mechanism of biologically important enzymes. The possibility of these analogs being developed as medicinal agents will also be investigated. Current interests concern an enzyme in the nucleic acid biosynthetic pathway, orotidine-5'-monophosphate decarboxylase
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Zeile, Jane B.S. (1973) Muhlenberg College, Chemistry Ph.D. (1977) Vanderbilt Univ., Chemistry At SFSU since 1983 Tel: 415. 338.7713 e-mail: jzeile@sfsu.edu |
Research Area: Transition Metal Organometallic Chemistry
The study of the active sites on heterogeneous catalysts and in biological molecules that are known to assist in the oxidation of alkanes. Synthesis and characterization by IR, NMR and UV VIS spectroscopy of new soluble transition metal complexes that model these active sites. Investigation of the effect of ligand size on electron transfer between the two or three metals present in each complex by electrochemical techniques. The development of 2D31P NMR of platinum phosphine dimers for the rapid determination of structure and coupling constants.
