Duke University
Biochemistry
Durham, NC

Overview
Duke is a private university that dates as a corporate entity from 1924; however, its roots go back to the Union Institute, founded in 1838. The graduate school has a faculty of more than 800. The campus is located on the edge of the Duke Forest, 8,500 acres of rolling, wooded land on the southwestern fringe of Durham. The proximity of all departments in the biological and basic medical sciences facilitates interdepartmental cooperation and results in a wide range of courses, research opportunities, and seminars. Duke has reciprocal arrangements with the University of North Carolina at Chapel Hill and North Carolina State University that allow students to enroll in courses at these nearby institutions.

There are approximately 5,200 graduate students enrolled at Duke University. The University Program in Biological Chemistry currently enrolls 23 students and supports 10 students.

The Location and Community
Durham is a city of some 200,000 people located in a metropolitan area of more than 1 million, midway between the Atlantic Ocean and the Appalachian Mountains. The climate is moderate, and the cultural life of the community is well developed. The University of North Carolina at Chapel Hill and North Carolina State University at Raleigh, the state capital, are nearby. Twelve miles away is the well-known Research Triangle Park of North Carolina, where a number of firms have large research establishments. The National Center for Health Statistics and the National Institute of Environmental Health Sciences are also located there. Many of the scientists employed by these organizations live in Durham and add to the scientific and cultural climate generated by the close relations between the universities. The weather is such that outdoor recreation is possible all year round.

Programs of Study and Degree Requirements
The University Program in Biological Chemistry is an interdisciplinary program offering a Certificate in Biological Chemistry. The Ph.D. is awarded by one of the five participating departments (biochemistry, biology, cell biology, chemistry, or pharmacology and cancer biology) from which the participating faculty members are drawn. Students may apply and be admitted directly to the program or apply to one of the participating departments with a request to be considered by the program. Students perform three research rotations with program faculty members, at least one of whom must be from the Medical Center (biochemistry, cell biology, or pharmacology) and one from the University (biology or chemistry). Students are encouraged to begin their rotations with an intensive, two-month summer rotation beginning in July. At the end of the first year, students select a mentor and a department in which to earn the Ph.D. degree.

The biological chemistry program is designed to provide training to students in the synthetic and mechanistic aspects of the interface between chemistry and biology. Specializations include carbohydrate, lipid, nucleic acid, and protein synthesis; molecular recognition between biomolecules; and mechanisms of catalytic processes involving proteins and nucleic acids and their associated cofactors. Course offerings, including a core focusing on the synthesis of biological macromolecules and mechanisms of enzymatic cofactors, are aimed at providing significant cross-training between chemistry and biology and developing a common language among students in different disciplines. Laboratory rotations begin in the summer and continue in the fall and (in some cases) spring semesters of the first year of study.

Facilities & Resources
The students have access to all of the research facilities of participating faculty members; the facilities are well funded and provide state-of-the-art equipment for magnetic resonance, mass spectrometry, and computing, among other areas.

Expenses and Aid
Tuition and fees total $34,074. Full-time Ph.D. students are charged a flat tuition rate each semester for six semesters, after which they are charged only registration and health fees. All of these fees are paid for by the program.

Financial Aid:
Students are usually supported for the first two years of graduate study by an NIH training grant and then through their adviser's department. Currently, 100 percent of the program students are receiving financial aid, including all tuition and fees, plus a stipend.

Housing/Living Expenses:
A wide variety of affordable housing arrangements are available to graduate students interested in locating housing in Durham near the Duke campus. The average cost of housing in University-owned apartments is $4700 per year.

How to Apply
Students may apply directly to the University Program in Biological Chemistry with the understanding that they will establish a departmental affiliation at the end of their first year. Students may also apply to any of the participating departments and indicate their interest in fulfilling the requirements for the Certificate in Biological Chemistry. Currently, the program does not have funding available for students who are not U.S. citizens. Students should apply using the online electronic application available on the graduate school's Web site (http://www.gradschool.duke.edu). All applications must be submitted by December 31

Who to Contact
Professor Johnnes Rudolph
Director of Graduate Studies
University Program in Biological Chemistry
Box 3567 DUMC
Durham, North Carolina 27710

Telephone: 919-681-8825

E-mail: blc@biochem.duke.edu

http://blc.duke.edu

The Faculty

• Michael Been, Professor (Biochemistry); Ph.D., Washington (Seattle), 1982. Cis- and trans-acting ribozymes from a human pathogen, hepatitis delta virus. Trends Biochem. Sci. 19:251-6, 1994.

• Patrick Casey, Professor (Pharmacology and Cancer Biology); Ph.D., Brandeis, 1986. Interaction of prenylcysteine methyl esters with the multidrug resistance transporter. J. Biol. Chem. 269:15973-6, 1994 (with Zhang, Sachs, Fine, and Casey).

• Allin Crumbliss, Professor (Chemistry); Ph.D., Northwestern, 1969. pH induced active ("uphill") liquid membrane transport of ferrioxamine B by the ionizable iophore lasalocid. Inorg. Chem. 38:3248, 1999 (with Spasojevic).

• Michael Fitzgerald, Assistant Professor (Chemistry); Ph.D., Wisconsin, 1994. A quantitative, high-throughput screen for protein stability. Proc. Nat. Acad. Sci. U.S.A. 97(15):8296-301, 2001 (with Ghaemmaghami).

• Katherine Franz, Assistant Professor (Chemistry); Ph.D., MIT, 2000. Pentacoordinate cobalt(III) thiolate and nitrosyl tropocoronand compounds. Inorg. Chem. 40:3774-80, 2001 (with Doerrer, Spingler, and Lippard).

• Timmothy Haystead, Associate Professor (Pharmacology and Cancer Biology); Ph.D., Dundee (Scotland), 1988. Smooth muscle myosin phosphatase-associated kinase induces Ca2+ sensitization via myosin phosphatase inhibition. J. Biol. Chem. 26:23441-6, 2002 (with Borman, MacDonald, Muranyi, and Hartshorne).

• Homme Hellinga, Assistant Professor (Biochemistry); Ph.D., Cambridge, 1986. Optimal sequence selection in proteins of known structure by simulated evolution. Proc. Natl. Acad. Sci. U.S.A. 91:5803-7, 1994 (with Richards).

• Tao-shih Hsieh, Professor (Biochemistry); Ph.D. Berkeley, 1977. Insertion mutagenesis of Drosophila Topoisomerase II: Probing the structure of eukaryotic topoisomerase II. J. Mol. Biol. 235:436-47, 1994 (with Lee and Linker).

• Thomas McIntosh, Associate Professor (Cell Biology); Ph.D., Carnegie-Mellon, 1973. Experimental tests for thermally-induced fluctuations in lipid bilayers. Progress Colloid Polymer Sci. 103:95-106, 1997 (with Simon).

• Paul Modrich, J. B. Duke Professor of Biochemistry and the Howard Hughes Institute; Ph.D., Stanford, 1973. Mismatch repair proteins mutS and mutL inhibit RecA-catalyzed strand transfer between diverged DNAs. Proc. Natl. Acad. Sci. U.S.A. 91:3238-41, 1994 (with Worth, Clark, and Radman).

• Christopher Newgard, Professor (Pharmacology and Cancer Biology); Ph.D., Texas Southwestern Medical Center, 1984. ®MD+SU¯13®MD-SU¯C NMR isotopomer analysis reveals a connection between pyruvate cycling and glucose-stimulated insulin secretion. Proc. Natl. Acad. Sci. U.S.A. 99:2708-13, 2002 (with Lu et al).

• Michael Pirrung, Professor (Chemistry); Ph.D., Berkeley, 1980. Kinetic mechanism and reaction pathway of T. thermophilus isopropylmalate dehydrogenase. J. Org. Chem. 59:2423, 1994 (with Han and Nunn).

• Christian Raetz, G. B. Geller Professor and Department Chairman (Biochemistry); Ph.D./M.D., Harvard, 1973. Bacterial endotoxins: Extraordinary lipids that activate eukaryotic signal transduction. J. Bacteriol. 175:5745-53, 1993.

• Johannes Rudolph, Assistant Professor (Biochemistry); Ph.D., MIT, 1993. Investigation of the specificity of natural and artificial substrates for human Cdc25A. Anal. Biochem. 289:43-51, 2001 (with Chen).

• B. Ramsay Shaw, Professor (Chemistry); Ph.D., Washington (Seattle), 1973. Bisulfite induces tandem double CC-TT mutations in double-stranded DNA. 2 kinetics of cytosine deamination. Biochem. 33:4121-9, 1994 (with Chen and Shaw).

• James Siedow, Professor (Biology); Ph.D., Indiana, 1973. Regulation of alternative oxidase kinetics by pyruvate and intermolecular disulfide bond redox status in soybean seedling mitochondria. FEBS Lett. 348:181-4, 1994 (with Umback and Wiskich).

• Eric Toone, Professor (Chemistry); Ph.D., Toronto, 1988. Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli. Structure 9:1-9, 2001 (with Mehta et al.).

• Ross Widenhoefer, Assistant Professor (Chemistry); Ph.D., Wisconsin-Madison, 1994. Enantioselective diene cyclization/hydrosilylation catalyzed by optically pure palladium bisoxazoline and pyridine-oxazoline complexes. J. Org. Chem. 65:3836-45, 2000 (with Perch and Pei).

• John York, Associate Professor (Pharmacology and Cancer Biology); Ph.D., Washington (St. Louis), 1993. Specificity determinants in phosphoinositide dephosphorylation: Crystal structure of an archetypal inositol polyphosphate 5-phosphatase. Cell 105:379-89 2001.

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