Grad Profiles - Tulane University Biochemistry

Overview
Tulane University was founded in 1834. Eleven academic divisions now enroll about 12,400 students. In addition to having one of the finest and most diverse academic curricula in the South, Tulane University and the city of New Orleans offer many cultural programs, including theater, opera, art exhibits, concerts, and outstanding lecture series by distinguished visitors.

Approximately 4,900 graduate students are enrolled at Tulane. Of these, about 100 are in the basic medical sciences, and about 15 to 20 are in biochemistry. The department generally has 6 to 8 postdoctoral fellows, who augment the research training of graduate students in biochemistry. The size of the graduate program allows personalized attention, maximum student-faculty interactions, and tutorials as well as lecture courses.

The Location and Community
New Orleans offers the advantages of a major cosmopolitan city and a distinctive mixture of cultural and recreational activities. The ambience of the old French Quarter and Uptown Garden District plus the Cajun culture and two-week-long Mardi Gras festivities are unique in the United States. Furthermore, New Orleans is an attractive place to live because of its housing affordability and ease of commuting from various parts of the city and surrounding suburbs.

Programs of Study and Degree Requirements
The Department of Biochemistry offers programs of study leading to the Ph.D. and M.S. degrees. Entering students usually have a B.S. degree with solid preparation in biochemistry, molecular and cellular biology, genetics, chemistry, physics, and mathematics. After a core curriculum is completed during the first year, students' programs of study are individually developed to meet their specific interests and may include courses in other basic science disciplines. The goal of the Ph.D. program is to develop highly competent scientists with the ability to conduct independent research in academic or other environments. The department has undergone major expansion over the last few years, including renovations of the physical facilities, development of modern shared instrumentation facilities for molecular biology, and recruitment of new faculty members.

The Ph.D. Program in Biochemistry provides lecture and tutorial courses, seminars, laboratory rotations, and major research projects carried out under the supervision of faculty research advisers. By the end of the second year of training, each student must demonstrate a comprehensive knowledge of biochemistry and molecular biology by successfully completing a qualifying examination. The doctoral degree is awarded following the formal presentation and defense of the dissertation research. There is no foreign language requirement. Normally four years are required to complete the Ph.D.

Facilities & Resources
The Department of Biochemistry is housed in the School of Medicine, which is located in a large medical complex. Faculty members have research laboratories that are well equipped for modern biochemistry and molecular biology research. There are also major shared instrumentation facilities and cooperative research efforts between faculty members in many basic science and clinical departments of the University as well as at the Tulane Regional Primate Center.

Expenses and Aid
Tuition payments are generally covered by tuition scholarships.

Financial Aid:
Stipends (at least $19,000 per year) and tuition scholarships are provided by the University or the department.

Housing/Living Expenses:
The School of Medicine maintains an apartment complex within walking distance of the campus; the average monthly rent for a shared double room in 2005-06 was $745 per person. Most students live in apartments, many of which are available off campus. The cost of living in New Orleans is relatively low for a large metropolitan area.

How to Apply
Applicants for admission are expected to have a strong educational background in biochemistry, molecular biology, and chemistry. Admission is based on the student's performance in undergraduate studies, scores on the Graduate Record Examinations, and letters of recommendation. A bachelor's degree with a major in biochemistry, biology, genetics, or chemistry from an accredited college or university is a prerequisite. Adequate TOEFL scores are required of students from countries in which English is not the native language.

Who to Contact

Graduate Studies Committee
Department of Biochemistry SL43
Tulane University Health Sciences Center
1430 Tulane Avenue
New Orleans, Louisiana 70112

504-588-5291

Fax: 504-584-2739

E-mail: thills@tulane.edu

http://www.tulane.edu

The Faculty

• Melanie Ehrlich, Professor; Ph.D., SUNY at Stony Brook, 1970. Gene expression and DNA-binding proteins; DNA rearrangements accompanying oncogenic transformation; DNA methylation and stability of human chromosomes.

• Jim D. Karam, Professor and Chair; Ph.D., North Carolina at Chapel Hill, 1965. RNA-binding proteins and control of DNA replication.

• Samuel J. Landry, Associate Professor; Ph.D., LSU, 1988. Protein folding; protein-protein interactions; antigen processing.

• Su-Chen Li, Research Professor; Ph.D., Oklahoma, 1966. Catabolism of glycoconjugates.

• Yu-Teh Li, Professor; Ph.D., Oklahoma, 1963. Chemistry and chemical pathology of glycoconjugates.

• Arthur J. Lustig, Associate Professor; Ph.D., Chicago, 1981. Role of telomere dynamics in chromosome stability and transcriptional regulation.

• James M. Nolan, Assistant Professor; Ph.D., Duke, 1988. Ribozyme structure-function and RNA-protein interactions.

• Joseph Vaccaro, Assistant Professor; Ph.D., Johns Hopkins, 1995. Molecular mechanisms of signaling and viral replication.

• William C. Wimley, Assistant Professor; Ph.D., Virginia, 1990. Folding and structure of proteins in membranes.

• Selected Publications of the Faculty

• Mahimkar, R. M., and W. H. Baricos et al. Identification, cellular distribution, and potential function of the metalloprotease-disintegrin MDC9 in the kidney. J. Am. Soc. Nephrol. 11:595-603, 2000.

• Jiang, G., et al. (M. Ehrlich). Provides only limited selectivity for CML cells and treatment might be complicated by silent BCR-ABL genes. Cancer Biol. Ther. 103-8, 2003.

• Ehrlich, M. Expression of various genes is controlled by DNA methylation during mammalian development. J. Cell. Biochem. 899-910, 2003.

• Ehrlich, M., et al. Satellite DNA hypomethylation in karyotyped Wilms tumors. Cancer Genet. Cytogenet. 97-105, 2003.

• eds. C. A. Pickover and S. K. Tewksbury. Scientific Visualization series (vol. 3). New York: John Wiley, 1994.

• Petrov, V., and J. D. Karam. RNA determinants of translational operator recognition by the DNA polymerases of bacteriophages T4 and RB69. Nucleic Acids Res. 3341-8, 2002.

• Bebenek, A., et al. (J. D. Karam). Dissecting the fidelity of bacteriophage RB69 DNA polymerase: Site-specific modulation of fidelity by polymerase accessory proteins. Genetics 162:1003-18, 2002.

• Petrov, V. M., S. S. Ng, and J. D. Karam. Protein determinants of RNA binding by DNA polymerase of the T4-related bacteriophage RB69. J. Biol. Chem. 277:33041-8, 2002.

• Landry, S. J. Structure and energetics of an allele-specific genetic interaction between DnaJ and DnaK: Correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK. Biochem. 42:4926-36, 2003.

• Wittung-Stafshede, P., J. Guidry, B. E. Horne, and S. J. Landry. The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70. Biochem. 42:4937-44, 2003.

• Carmicle, S., G. Dai, N. K. Steede, and S. J. Landry. Proteolytic sensitivity and helper T-cell epitope immunodominance associated with the mobile loop in Hsp10s. J. Biol. Chem. 277:155-60, 2002.

• Dai, G., S. Carmicle, N. K. Steede, and S. J. Landry. Structural basis for helper T-cell and antibody epitope immunodominance in bacteriophage T4 Hsp10: Role of disordered loops. J. Biol. Chem. 277:161-8, 2002.

• Ashida, H., K. Maskos, S.-C. Li, and Y.-T. Li. Characterization of a novel endo-β-galactosidase specific for releasing the disaccharide GlcNAc-∝-1,4Gal from glycoconjugates. Biochem. 41:2388-95, 2002.

• Li, S.-C., Y.-T. Li, S. Moriya, and T. Miyagi. Degradation of G(M1) and G(M2) by mammalian sialidases. Biochem. J. 360:233-7, 2001.

• Ashida, H., et al. (S.-C. Li and Y.-T. Li). A novel endo-β-galactosidase from Clostridium perfringens that liberates the disaccharide GlcNAc-∝-l,4Gal from glycans specifically expressed in the gastric gland mucous cell-type mucin. J. Biol. Chem. 276:28226-32, 2001.

• Li, Y.-T., et al. (S.-C. Li). Association of GM4 ganglioside with the membrane surrounding lipid droplets in shark liver. J. Lipid Res. 43:1019-25, 2002; (erratum in: J. Lipid Res. 44:437, 2003).

• Lustig, A. J. Perspective: Does telomere rapid deletion in yeast hold clues to catastrophic telomere loss in mammals. Nat. Rev. Gen. 4, in press.

• Williams, B., and A. J. Lustig. The paradoxical relationship between NHEJ and telomeric fusion. Mol. Cell. 11:1125-6, 2003.

• Wyatt, H. R., H. Liaw, G. R. Green, and A. J. Lustig. Multiple roles for saccharomyces cerevisiae histone H2A in telomere position effect, Spt phenotypes, and double-strand-break repair. Genetics 164:47-64, 2003.

• Bucholc, M., Y. Park, and A. J. Lustig. Intrachromatid excision of telomeric DNA as a mechanism for telomere size control in Saccharomyces cerevisiae. Mol. Cell. Biol. 21:6559-73, 2001.

• Rasmussen, T. A., and J. M. Nolan. G350 of Escherichia coli RNase P RNA contributes to Mg binding near the active site of the enzyme. Gene 10:177-85, 2002.

• Sharkady, S. M., and J. M. Nolan. Bacterial ribonuclease P holoenzyme crosslinking analysis reveals protein interaction sites on the RNA subunit. Nucleic Acids Res. 29:3848-56, 2001.

• Ray, A. S., et al. (J. A. Vaccaro). Probing the molecular mechanisms of AZT drug resistance mediated by HIV-1 reverse transcriptase using a transient kinetic analysis. Biochem. 42:8831-41, 2003.

• Vaccaro, J. A., K. M. Parnell, S. A. Terezakis, and K. S. Anderson. Mechanism of inhibition of the human immunodeficiency virus type 1 reverse transcriptase by d4TTP: An equivalent incorporation efficiency relative to the natural substrate dTTP. Antimicrob. Agents Chemother. 44:217-21, 2000.

• Wimley, W. C. The versatile beta-barrel membrane protein. Curr. Opin. Struct. Biol. 13:404-11, 2003.