A Degree Built By You
You’ll customize your plan of study with help from faculty advisors and your research mentors, choosing from a broad list of available courses in the biomedical science graduate curriculum. In the first 2 years of study, you are required to complete a minimum of 24 hours of graded coursework (including a total of 8 units of Independent Study Research), as well as at least 6 hours of ungraded coursework (typically met with the RCR training.) Note that students coming into the program from the Medical Scientist Training Program (MSTP) or with an MA/MS degree, may be exempt from the minimum graded coursework requirement.
Your Faculty Advisory Committee and Research Mentors play an important role in your graduate student career.
Faculty Advisory Committee
- Customizes your plan of study to include basic and advanced courses in and around your research focus.
- Aids in formulating research objectives and thesis topics for success in the Preliminary Qualifying Exam.
- Guides annual progress on your dissertation.
- Advises on the skills and experience you’ll need to reach your professional goals.
- Customize your plan of study with day-to-day troubleshooting and by developing a long-term thesis project.
- Informs you of different career opportunities.
- Promotes your presentations at local, national, and international meetings and workshops.
- Helps set and revise short- and long-term goals.
"While I was looking at graduate schools, Duke Biochemistry stood out because of its diverse blend of research and the amount of labs that matched my research interests. Plus, in reading the publications, I could see a high level of collaborations—something I’ve always looked forward to. It has been great to be part of this community; everyone is really helpful and I have seen myself grow immensely during my first year. "
—Akanksha Manghrani, 2018 Matriculant
First Year Schedule
The typical schedule for a first year biochemistry PhD consists of 2-3 classes and two seminar courses each semester. These core courses will give you the skills to:
- Demonstrate a firm grasp of the foundations of modern biochemistry.
- Critically analyze scientific literature.
- Orally present scientific findings.
- Conceive and write student fellowship applications.
The application period is now closed. Sign up here if you'd like to learn more about our program and research.
A Note About the GREs
This program does not require applicants to provide GRE (Graduate Record Examination) or other graduate entrance exam scores, but does allow you to upload scores if you feel they enhance your application. If you choose to submit test scores, you may enter them on the Test Scores page. If you choose to enter self-reported test scores, official test scores will become a required component of your application. The Admissions Committee of the Graduate Program in Biochemistry evaluates all candidates holistically, on the basis of academic performance, laboratory research experience, letters of recommendation, and a personal statement.
Fall and spring semester courses, of particular interest to Biochemistry students, are described below. Courses offered by other departments in the Basic Sciences can be found on the School of Medicine Biomedical Graduate Education website and in the Biochemistry Graduate Student Handbook.
BIOCHEM 593-01 - Independent Study (2 units) Graded
Fall and Spring Semesters (Years 1 and 2)
In year one, you will rotate through and conduct faculty/mentor-approved research in different Biochemistry labs. If you’re in your 2nd year, you’ll be in a thesis lab. Students are expected to be performing research when they are not in class, attend departmental seminars, keep up-to-date lab notebooks, and present oral and written summaries of their ongoing research, as appropriate for each laboratory.
BIOCHEM 622 (SBB 622) - Structure of Biological Macromolecules (3 Units)
You will learn how to get the most out of experimental and computational 3D structures including: a) 3D Molecular Literacy: Computer and physical molecular models of proteins and nucleic acids, worksheets, and hands-on exploration. b) Data bases and the data itself: gaining familiarity with the Protein Data Bank (PDB); the Electron Density Server (EDS); and the peculiarities, caveats, and reliabilities of different categories of molecular data. c) Computational methods for studying and depicting macromolecules including: model building in structural biology; Molprobity and all-atom contact analysis and methodologies for multiple conformations, ensembles, and mobility. d) Projects include: interactive 3D illustration about macromolecules using kinemages or other molecular graphics programs, often with short, non-interactive introduction.
BIOCHEM 631 - Contemporary Topics in Membrane Biology (CMB631, NEURO631, PHARM631) (2 Units)
Instructors: Lee, Bennett, Kuehn, Rajagopal, and Yang
2nd ½ Spring Semester
This course will highlight modern topics regarding biological membranes and membrane proteins that are important for human physiology and disease. Topics include structure and dynamics of biological membranes, structure and function of membrane proteins that play critical roles in cell signaling, diseases related to dysfunction of membrane and membrane proteins, and current efforts on drug discovery. Major techniques used in membrane research will also be covered. The format will be a combination of lectures and discussion of primary literature. Students will be evaluated based on their class participation and performance at the final presentations.
BIOCHEM 658 - Structural Biochemistry I (2 units) Graded
1st ½ Fall Semester
Structure of Macromolecules – This class teaches the principles of modern structural biology including protein-nucleic acid recognition, enzymatic reactions, viruses, immunoglobulins, signal transduction, and structure-based drug design—described in terms of the atomic properties of biological macromolecules. There will be discussions on the methods of structure determination, with particular emphasis on macromolecular X-ray crystallography, Nuclear Magnetic Resonance (NMR) methods, homology modeling, and bioinformatics. You will use molecular graphics tutorials and Internet databases to view and analyze structures.
BIOCHEM 659 - Structural Biochemistry II (2 units) Graded
2nd ½ Fall Semester
Molecular Biology I – As a continuation of BCH 658, this introductory course teaches how to use quantitative methods to understand biological structure and function. You’ll study the structure/function analysis of proteins as enzymes, kinetics of binding, catalysis and allostery, protein folding, stability, and design protein-protein interactions.
BIOCHEM 667 - Biochemical Genetics I (2 units) Graded
1st ½ Spring Semester
A major emphasis of this course is on the reading and in-depth discussion of primary research papers. You will explore how new nucleic acid biology concepts have been developed and what types of experiments have made advances possible. Each course section will consist of background lecture material presented by the faculty member, followed by several sessions to discuss paradigm papers selected by the faculty. You will do oral presentations using figures from the papers and explanatory background as needed and prepare an 8-10 page research paper or an oral talk to demonstrate proficiency in the topics of DNA and Genome Stability—Chromatin and chromosome structure, replication, repair, genetic recombination, mutation, and chromosome rearrangement.
BIOCHEM 668 – RNA Biology (3 units) Graded
This course explores various aspects of RNA biology and function. Topics include splicing, translation, RNA: Protein interactions, non-coding RNAs, RNA modifications, viral RNA regulation, RNA structure-function relationships, and RNA-targeted drug discovery. You will also learn about major techniques in RNA research, including in vitro and in vivo methods for understanding global RNA regulation. The format will be a combination of weekly lectures and discussion of primary scientific literature. You will be evaluated on your participation and performance during in-class presentations and will write a short mock research grant on a topic of your choosing.
BIOCHEM 681 – Biophysical Methods (3 units) Graded
You’ll survey the theory and application of biological techniques—based on physical principles—to understand their application in primary scientific literature. Methods covered include: Optical Spectroscopy, Fluorescence, Binding, Light Microscopy, Electron Microscopy, Hydrodynamics, Kinetic Methods, Electrophysiology, Magnetic Resonance and Mass Spectrometry. Lectures on each method are presented by an expert.
BIOCHEM 690 – Advanced Topics in Biochemistry- High Resolution CRYO-EM Image Analysis (3 units) Graded
This Advanced Topics course will focus on the image analysis aspects of cryo-electron microscopy (EM), including image enhancement, reconstruction, classification and movie processing used to determine the high-resolution structure of proteins from cryo-EM images. The course will provide an overview of the cryo-EM structure determination pipeline, focusing primarily on the data analysis aspects of the technique and covering the full breadth of reconstruction strategies. Prerequisites: Students should have background in either protein structure/molecular biology or computer vision/image processing.
BIOCHEM 695 – Understanding NMR Spectroscopy (4 units) Graded
Spring Semester (alternating years with BCH 696)
Aimed for students with some familiarity with high-resolution NMR, you will deepen your understanding of how NMR experiments actually work and be introduced to quantum mechanical tools that help explain pulse sequences. You’ll study advanced biomolecular NMR experiments that enable the structural and dynamic characterization of biomolecules. Roughly half the course follows online lectures that accompany the textbook, with class meetings emphasizing concepts, group discussion, and problem solving. Instructor consent is required.
BIOCHEM 696 – Macromolecular crystallography (4 Units)
Instructor: Schumacher and Staff
Spring Semester (alternating years with BCH 695)
This course teaches the theoretical and practical principles of macromolecular X-ray crystallography. Topics include crystal symmetry, space group theory and determination, diffraction theory, a practical understanding of crystallization, X-ray intensity data collection and data processing, phase determination, and refinement and model validation.
BIOCHEM 745S/746S – Biochemistry Seminar (1 unit) Graded
This course is a requirement of all first, second & third year biochemistry graduate students to learn how to clearly and concisely present the background, data, conclusions, and future prospects of your research in both oral and written formats. First year students will present their rotation projects. Second and third year students will annually present their research. All students will provide feedback so each presenter can improve presentation content and style.
BIOCHEM 790S – Seminar (Topics) (2 units) Graded
This is a discussion-based course that includes introductory lectures and the critical reading of select topics in Biochemistry literature. Topics and instructors are announced each semester.
BIOLOGY 701 – Succeeding in Graduate School in the Biological Sciences (0.5 units) CR/NC
1st ½ Fall Semester
This course is a great introduction to understanding the graduate student mindset. Weekly talks and Q&As will focus on choosing a thesis advisor, writing a grant proposal, the scientific manuscript peer review processes, and other topics related to transitioning to and being successful in graduate school.
BIOLOGY 702 – Succeeding Beyond Graduate School - Career Options with a PhD in the Biological Sciences (0.5 units) CR/NC
2nd ½ Fall Semester
You’ll attend weekly lectures and Q&As on alternative careers in the biological sciences, preparing for job applications, and other topics related to succeeding beyond graduate school.
SBB 546S – Structural Biology and Biophysics (SBB) Seminar (1 unit) Graded
Fall and Spring Semester
Each week, a student will present a paper on their research. Attendance is open to all graduate and postdoctoral students and faculty who have an interest in structural biology. All SBB certificate students are required to attend.
BIOCHEM 536 (CHEM 536) - Bioorganic Chemistry (4 Units) Graded
This course covers basic enzymology, mechanisms of enzymatic reactions, cofactors, oxidoreductases, C1 chemistry, carbon-carbon bond formation, carboxylation/decarboxylation, heme, pyridoxal enzymes, and thiamine enzymes.
BIOCHEM/CBI 761 (CELLBIO 761) – Cellular Signaling Module I: GPCR Signaling and Disease (1 Unit) Graded
First 1/3 Spring Semester
This module covers the basic mechanism of signal transduction through G protein coupled receptors (GPCR) and how they control a wide array of biological functions—from vison to reproduction—and how they are the largest targets of therapeutic interventions. You will study how new concepts of signal transduction mechanisms are leading to the development of new and improved therapies for various disorders.
BIOCHEM/CBI 762 (CELLBIO 762) – Cellular Signaling Module II: Intracellular Signaling and Disease (1 Unit) Graded
Mid 1/3 Spring Semester
This module covers how ion channels and intracellular nuclear receptors control cellular functions, mediated through transcription or calcium signaling, to regulate physiological processes in health and disease.
BIOCHEM/CBI 763 (CELLBIO 763) – Cellular Signaling Module III: Growth Factor Pathway in Development and Disease (1 Unit) Graded
Last 1/3 Spring Semester
This module focuses on signaling pathways induced by extracellular factors that regulate growth, survival, and development—and their deregulation in diseases including cancer. Topics include those regulated by ligand-activated Receptor Tyrosine Kinases, Wnt/beta-catenin signaling, Notch signaling, and Hedgehog signaling.