Provisional University Bulletin (2026-2027)

• Master of Science
• Doctor of Philosophy

Master of Science in Biochemistry and Biophysics

The graduate program in Biochemistry and Biophysics, leading to the degree of Master of Science, is designed to give students a substantial understanding of the chemical and physical molecular events in biological processes and experience in research. The program is divided between formal course work, and practical training in biochemical and biophysical techniques, and a research project. Additional courses and seminars are available in a wide range of subjects.

Doctor of Philosophy in Biochemistry and Biophysics

The graduate program in Biochemistry and Biophysics, leading to the degree of Doctor of Philosophy, is designed to provide students with a deep understanding of the mechanisms governing the workings of biological macromolecules. The emphasis in the graduate program is placed upon experimental and computational studies to train students to carry out independent original research. Students are required, however, to complete formal course work in areas including advanced biochemistry, physical biochemistry and biophysics. Additional courses and seminars are available that cover a wide range of subjects, including enzyme regulation and mechanism, neurobiology, structural biology (including protein crystallography, magnetic resonance spectroscopy, electron microscopy, and computational structural biology), membrane biology, molecular microscopy, biophysical chemistry, neuroscience, sensory transduction, protein evolution, and statistical, machine learning, and other computational methods.

Applicants are expected to have strong backgrounds in the physical sciences with undergraduate majors in any related field, such as biochemistry, biology, biophysics, chemistry, engineering, mathematics, or physics. Research for the PhD dissertation is carried out under the personal supervision of a faculty adviser; advisers can be from any department within the Division of Science. Prospective applicants should obtain the current list of Training Faculty and their research interests and recent publications from the program or view this information on the program website.

All students are required to carry out an original independent research project in the laboratory of a Brandeis faculty member, including writing a PhD dissertation that constitutes a substantial contribution to the field of research.

All students participate in full-time summer research.

Master of Science in Biochemistry and Biophysics

Knowledge

All students graduating with a Biochemistry and Biophysics MS degree should have knowledge of the following general areas:

1. Firm understanding of general chemistry and organic chemical reaction mechanisms, particularly in the area of carbonyl chemistry.
2. Molecular forces determining protein and nucleic acid folding and membrane assembly.
3. Mechanisms by which enzymes catalyze cellular chemical reactions.
4. Strategies by which cells store and transmit information in DNA and RNA.
5. Mechanisms for communicating changes in the extracellular environment to the cell's interior.
6. Techniques for determining molecular structures of macromolecules.
7. Relation of impairment in macromolecular function to disease.

Core Skills

Our MS program requires students to use a set of basic skills to address problems particular to biochemistry, some of which should be mastered through prerequisites taken prior to encountering our introductory course. The core skills needed are:

1. Facility with familiar mathematical functions, proficiency in univariate calculus, and understanding of basic elements of probability and statistics.
2. Familiarity with the application of calculus to problems in classical physics.
3. Mastery of basic principles of equilibrium thermodynamics and chemical kinetics.
4. Ability to read and analyze primary research literature.

Doctor of Philosophy in Biochemistry and Biophysics

Knowledge

1. The PhD program is designed to provide students with a deep understanding of the mechanisms governing the workings of biological macromolecules in terms of the principles of chemistry and physics.
2. The curriculum provides advanced education in the principles and study of macromolecular chemistry, mechanism, evolution, and structure.
3.  Lecture courses emphasize understanding the relationships between macromolecular structure, dynamics, and function.
4. Advanced seminar and small-lecture classes emphasize analyzing primary literature in specialized topics.

Core Skills

1. Emphasis in the PhD program is placed on experimental/computational research work to train students to carry out independent original research.
2. Students are trained to use tools of mathematics and physics to engage with problems arising in the behavior of proteins, nucleic acids, and membrane assemblies.
3. Students are given numerous opportunities to practice conveying scientific information via expository writing and public speaking.
4. Students are encouraged to attend and present research results at professional scientific meetings.
5. Trainees are required to propose and defend – orally and in writing – two research projects of their own choice, as models for writing grant applications and other kinds of research proposals.

The general requirements for admission to the Graduate School are listed in an earlier section of this Bulletin. For specifics of the program’s requirements, please see the program website.

Niels Bradshaw
(Biochemistry)


Carol Fierke
(Biochemistry)

Jeff Gelles
(Biochemistry)

Alex Johnson
(Biochemistry; Volen Center)

Julia Kardon
(Biochemistry)


Jane Kondev
(Physics)

Mike Marr
(Biology; Rosenstiel Center)

Daniel Oprian
(Biochemistry (Neuroscience; Volen Center)

Maria-Eirini Pandelia
(Biochemistry; Rosenstiel Center)

Timothy Street
(Biochemistry; Biology; Rosenstiel Center)

Douglas Theobald
(Biochemistry)

Hyunjun Yang
(Biochemistry)

Alexandre Bisson (Biology; Rosenstiel Center)
Cellular organization and behavior in the Archaea domain of life.

Niels Bradshaw (Biochemistry)
Regulation of Protein Phosphatases and the Evolution of Cellular Signaling.

Guillaume Duclos (Physics)
Self-organization of living and active matter.

Irving Epstein (Chemistry; Neuroscience; Volen Center)
Oscillating chemical reactions and pattern formation in reaction-diffusion systems. Mathematical modeling of biochemical kinetics and neural systems. 

Thomas Fai (Mathematics; Volen Center)
Scientific computing, fluid dynamics, and mathematical biology.

Carol Fierke (Biochemistry)
Enzymology and biochemistry of medically important processes, including post-translational modification, amyloid formation (amylin) and metalloregulation.

Seth Fraden (Physics)
Macromolecules in suspension. Physics of protein crystallization. Microfluidics.

Jeff Gelles (Biochemistry)
Single-molecular biochemistry and biophysics. Transcription and RNA processing. Cytoskeletal networks and regulation.

Bruce Goode (Biology; Rosenstiel Center)
Cytoskeletal mechanisms controlling cell morphogenesis.

Leslie Griffith (Biology; Neuroscience; Volen Center)
Biochemistry of behavior.

Michael Hagan (Physics)
Application of statistical mechanics, modern computational techniques, and theory to problems in biology and condensed matter physics; assembly of viral capsids and other large protein complexes; pattern formation in collections of internally driven particles; effects of molecular chirality on large-scale structure

Lizbeth Hedstrom (Biology; Chemistry)
Design of targeted protein degraders; antibiotic discovery; enzyme structure-function studies.

Sebastian Kadener (Biology; Neuroscience; Rosenstiel Center; Volen Center)
Molecular neurobiology and RNA metabolism.

Julia Kardon (Biochemistry)
Mechanisms for control of mitochondrial protein activity, quality, and lifespan.

Jane Kondev (Physics)
Condensed matter theory and quantitative biology; application of condensed matter physics models to problems in molecular and cell biology such as regulation of gene expression and chromosome structure.

Isaac Krauss (Chemistry)
Chemical glycobiology and organic chemistry.

Susan Lovett (Biology; Rosenstiel Center)
Genetics and molecular biology of bacteria and yeast.

Mike Marr (Biology; Rosenstiel Center)
Gene expression in cellular stress responses.

Josh Meisel (Biology; Rosenstiel Center)
Mitochondrial genetics and metabolism in health and neurodegenerative disease.

Daniel Oprian (Biochemistry (Neuroscience; Volen Center)
Structure-function studies of visual pigments and other cell surface receptors.

Maria-Eirini Pandelia (Biochemistry; Rosenstiel Center)
Mapping the functional repertoire of (bio)inorganic systems and protein metallocofactors; paradigms of (bio)catalysts relevant to the human health and environment.

Thomas Pochapsky (Chemistry; Rosenstiel Center)
Biological redox enzymes structure and mechanism.

Kaushik Ragunathan (Biology)
Molecular mechanisms of epigenetic inheritance; single molecule approaches to study chromatin associated factors in vitro and in cells.

Avital Rodal (Biology; Rosenstiel Center; Volen Center)
Endosomal membrane traffic in neurons.

Ben Rogers (Physics)
Self-assembly at the colloidal length scale.

Klaus Schmidt-Rohr (Chemistry)
Solid-state NMR and structure determination of complex materials, including fuel-cell membranes, semicrystalline polymers, carbon materials, nanocomposites, natural organic matter, and thermoelectrics; NMR technique development; basic thermodynamics.

Timothy Street (Biochemistry; Biology; Rosenstiel Center)
Mechanisms of protein folding in the cell.

Douglas Theobald (Biochemistry)
Evolution, structure, and function of macromolecular complexes.

Chi Ting (Chemistry)
Total synthesis of natural products. Chemoselective functionalization of peptides. Genome mining and natural product biosynthesis.

Bing Xu (Chemistry)
New molecular materials and nanomaterials for the exploration in biomedicine (e.g., molecular drug delivery, cancer therapy, biomedical diagnostics, and biomimetics) and other fundamental problems in nanoscience and biological science.

Hao Xu (Chemistry)
Non-precious metal catalysis directed towards organic synthesis.  Translational synthetic chemistry.  Discovery of new disease targets and therapeutic probes in human biology.

Hyunjun Yang (Biochemistry; Volen Center)
De novo Protein Design and Supramolecular Assemblies

Hannah Yevick (Physics)
Mechanics of cell and tissue development, collective behaviors in living systems.

Program of Study

The MS program in Biochemistry and Biophysics is a two-semester program, designed to accommodate students with previous academic majors in a wide range of fields, including biology, biochemistry, physical chemistry, engineering, and physics. The required program of study consists of:

1. Eight one-semester courses, all completed with a grade of B- or higher:
   • BCHM 101a Advanced Biochemistry: Enzyme Mechanisms
   • BCHM 103b Advanced Biochemistry: Cellular Information Transfer Mechanisms
   • BCHM 104b Physical Chemistry of Macromolecules II
   • One other advanced level course from the School of Science, approved in advance by the Director of Graduate Studies.
   • Research Requirement: BCBP 297a/b Master's Lab Research or BIOL 251a Project Laboratory in Protein Biochemistry
   • BIOL 205 Masters Proseminar
   • BCBP 350a and 350b Biochemistry and Biophysics Research Seminar

In order to earn a degree from this program, the student must complete a minimum of 32 credits.

With approval of a supervising faculty member (chosen from the training faculty) and the Director of Graduate Studies, students have the option to write a Master’s Thesis (BCBP 299a) following completion of at least one full semester of Master’s Lab Research (BCBP 297a and/or 297b), provided that the research was performed in a single laboratory at Brandeis. Those who wish to complete a Master's Thesis in their third or fourth semester must obtain approval by March 1st of their second semester (for students who matriculate in the fall) or by November 1st (for students who matriculate in the spring).

At the discretion of the Director of Graduate Studies, students may be asked to leave the program at the end of a semester if they are found to be not making satisfactory progress toward attaining the M.S. degree. Satisfactory progress includes completing all required courses with grades of B- or higher and, for students engaged in thesis research, demonstrating adequate research progress thereafter as determined by the student’s graduate committee. 

Residence Requirement

The in-person residence requirement is two semesters.

Language Requirement

There is no language requirement.

Program of Study

A. Lecture/Seminar Course Requirement

Students working toward the PhD degree must complete six one-semester lecture or seminar courses with a grade of B- or higher. Four of these courses are required and must be completed during the student’s first year in the program. Ordinarily, the four required first year courses are: BCHM 101a, BCHM 102a, BCHM 104b, and BCBP 200b. However, with the prior approval of the Director of Graduate Studies, other courses can be substituted for BCHM 101a, BCHM 102a, and/or BCHM 104b in order to tailor the program of required courses to the academic needs and interests of the particular student. In addition to the four required first-year lecture/seminar courses, students must also take two additional elective lecture/seminar courses during their time in the program.  All electives must be approved by the Director of Graduate Studies.

B. Research Training Courses

In addition to the lecture/seminar course requirements described above, all students must enroll in research training by registering for courses as described here: (1) In the first year, students must register for two semesters of laboratory rotations (BCBP 300a and 300b). In each semester students do two rotations, for a total of four in their first year. All students beyond the first year must register for BCHM 401d every semester.

C. Student Talks

During their second year and beyond, each student must present their own research progress at least once a year in the BCBP/MSM Student Talk series.

D. Progress Meetings

Students in their third and higher years of study will have yearly (or more often) progress meetings with a committee of three or more faculty, including the student’s dissertation advisor, for the purpose of helping the student maintain a satisfactory trajectory toward completion and defense of the dissertation. These meetings must be documented with a form signed by the thesis committee members and turned into the Division of Science Graduate Affairs Office by the student.

E. Responsible Conduct of Research Training

All students must complete training in Responsible Conduct of Research as specified by the university and the program.

Teaching Requirement

All PhD students are required to participate in undergraduate teaching during the course of their studies. Every graduate teaching assistant (TA) is supervised by a member of the faculty, who serves as a mentor to improve the quality of the TA's teaching. Please see the GSAS section on Teaching Requirements and the program handbook for more details.

Residence Requirement

The minimum in-person residence requirement is three years.

Language Requirement

There is no language requirement.

Qualifying Examinations

To qualify for the PhD degree, each student must write and defend in oral examinations two propositions related to research in biochemistry and/or biophysics. One of these will be in the general area of the student's thesis research, while the other will be unrelated to this area.

Summer Registration

PhD students are required to be on campus or at a related lab for the full year. During the summer term students will be enrolled in CONT 250b by the Registrar's office. Registration for Graduate Summer Term does not count toward the residency requirement. The summer registration fee will be waived.

Dissertation and Defense

The dissertation must report the results of an original scientific investigation into an approved subject and must demonstrate the competence of the PhD candidate in independent research. The dissertation research must be presented and defended in a final oral examination.

Program of Study

Students wishing to obtain this specialization must first gain approval of the Director of Graduate Studies or quantitative biology liaison. This should be done as early as possible--ideally, during the first year of graduate studies. In order to receive the PhD in Biochemistry and Biophysics with additional Specialization in Quantitative Biology, candidates must complete the requirements for the PhD described above and the course requirements for the Quantitative Biology specialization that are described in the Quantitative Biology section of this Bulletin.

Any alteration to the Quantitative Biology course requirements must be approved by the Director of Graduate Studies and by the Quantitative Biology program faculty advisory committee.

Every student, whether or not currently in residence, must register at the beginning of each term. All graduate students will be evaluated by the program each spring. At this evaluation the records of all graduate students will be carefully reviewed with reference to the timely completion of coursework and non-course degree requirements, the quality of the work and research in progress and the student’s overall academic performance in the program. Progress will be reviewed by the Graduate Committee at the end of each year, and a student may be asked to leave the program if their progress is found to be unsatisfactory.

To advance into the second year of graduate studies, students must earn grades of B- or better in all courses, including rotations, and have gained a position by mutual consent of the student and research advisor in a research group at Brandeis in which the thesis research is to be carried out. To advance into the third year of the program, students must have grades of B- or better in all courses, have performed satisfactorily on research propositions, and be in good standing in the thesis research laboratory. Once thesis work has begun, students meet at least once per year with their Progress Meeting Committee, which includes the thesis adviser and at least two other professors, to discuss progress toward the completion of the dissertation research.

BCHM 100a Advanced Introductory Biochemistry
[ qr sn ]

Prerequisite: One year of organic chemistry with laboratory.

Topics include protein and nucleic acid structure; chemical basis of enzyme-catalyzed reaction mechanisms and enzyme kinetics; the chemical logic of metabolic pathways, including glycolysis and oxidative phosphorylation; and regulation of enzymatic pathways through allosteric control. Usually offered every year in multiple sections.

BCHM 101a Advanced Biochemistry: Enzyme Mechanisms
[ sn ]

Prerequisites: One year of organic chemistry with laboratory and BCHM 100a or equivalents.

Describes the principles of biological catalysts and the chemical logic of metabolic pathways. Discusses representative enzymes from each reaction class, with an emphasis on understanding how mechanisms are derived from experimental evidence. Topics include serine proteases, phosphatases, isomerases, carboxylases, and dehydrogenases. Usually offered every year.

BCHM 102a Quantitative Approaches to Biochemical Systems
[ dl sn ]

Prerequisite: BCHM 100a or equivalent and Math 10a and b or equivalent.

Introduces quantitative approaches to analyzing macromolecular structure and function. Emphasizes the use of basic thermodynamics and single-molecule and ensemble kinetics to elucidate biochemical reaction mechanisms. Also discusses the physical bases of spectroscopic and diffraction methods commonly used in the study of proteins and nucleic acids. Usually offered every year.

BCHM 103b Advanced Biochemistry: Cellular Information Transfer Mechanisms
[ oc sn ]

Prerequisites: One year of organic chemistry with laboratory and BCHM 100a or equivalents. BIOL 14a or the equivalent is recommended.

Molecular mechanisms of information transfer in biological systems. Topics include nucleic acid biochemistry, processing of genetic information, and signal transduction. Each section will focus on the chemistry and regulation of a selected example from these fundamental processes. Lectures will be complemented by reading assignments and student presentations on articles from the original research literature. Usually offered every year.

BCHM 104b Physical Chemistry of Macromolecules II
[ dl sn ]

Prerequisites: BCHM 100a, and one of the following: BCHM 104a, CHEM 141a, or Phys 40a, and Math 10a and b or equivalent.

Illustrates the basic principles on which biological macromolecules are constructed and by which they function. Describes overall structures of proteins, nucleic acids, and membranes in terms of the underlying molecular forces: electrostatics, hydrophobic interactions, and H-bonding. The energetics of macromolecular folding and of the linkage between ligand binding and conformational changes will also be discussed. Recitation optional. Usually offered every year.

BCBP 200b Reading in Macromolecular Structure-Function Analysis

Introduces students to chemical and physical approaches to biological problems through critical evaluation of the original literature. Students analyze scientific papers on a wide range of topics in the fields of biochemistry and biophysics. Discussion focuses on understanding of the scientific motivation for and experimental design of the studies. Particular emphasis is placed on making an independent determination of whether the author's conclusions are well justified by the experimental results. Students are also introduced to grant-proposal writing by preparing NIH-format mock proposals for critical discussion and evaluation. Usually offered every year.

BCBP 240a Advanced Topics in Single-molecule Biophysics

Prerequisite: BCHM 102a or the equivalent.

Explores the use of single-molecule biophysics techniques to reveal the kinetics and mechanisms of biochemical reactions. This graduate-level advanced-topics course will cover statistical theory underlying single-molecule fluorescence experiments, computational methods used to analyze data, and practical aspects of experiment design. Usually offered every third year.

BCBP 296a Master's Lab Rotation I

Laboratory rotation courses for Master's students in Biochemistry and Biophysics. Enrollment by others requires permission of the Program Chair. Usually offered every year.

BCBP 297a Master's Lab Research I

Yields twelve semester-hour credits.

Laboratory research for Master's students in Biochemistry and Biophysics. Enrollment requires permission of the Program Chair. Usually offered every year.

BCBP 297b Master's Lab Research II

See description under BCBP 297a. Usually offered every year.

BCBP 299a Master's Thesis

Usually offered every year.

BCBP 300a Introduction to Research in Biochemistry and Biophysics I

BCBP 300a is a laboratory rotation course in which students gain direct experience conducting research in biochemistry and biophysics. Intended for Biochemistry and Biophysics graduate students; enrollment by others requires permission of the Program Chair. Usually offered every year.

BCBP 300b Introduction to Research in Biochemistry and Biophysics II

See description under BCBP 300a. Usually offered every year.

BCBP 350a Graduate Research Seminar

Seminar course for Biochemistry and Biophysics MS students. Enrollment by others requires permission of the Director of Graduate Studies.

Presents research on topics of current investigation in the field. Usually offered every year.

BCBP 350b Graduate Research Seminar

Seminar course for Biochemistry and Biophysics MS students. Enrollment by others requires permission of the Director of Graduate Studies.

Presents research on topics of current investigation in the field. Usually offered every year.

BCBP 401d Biochemical Research Problems

All graduate students beyond the first year must register for this course each semester.

Independent research for the MS and PhD degrees. Specific sections for individual faculty members as requested.

BIOL 205a Masters Proseminar

Enrollment limited to Life Science Masters students.

In the life sciences, theories, methods and discoveries must be communicated effectively. Equally important is the ability to interpret and evaluate the work done by others. Students will have opportunities to learn, practice and evaluate oral and written methods of scientific communication. Usually offered every year.

BIOL 251a Project Laboratory in Protein Biochemistry
[ sn ]

Features experiments in protein biochemistry that are fundamental to the field of biotechnology. These include protein purification, characterization and quality assessment. Focus is placed on designing purification protocols for both tagged and untagged proteins using biochemical knowledge. The designed protocols are tested by purifying known proteins. As part of the course, students will contribute to research projects of unknown outcome by purifying and assaying novel proteins. Usually offered every year.

CBIO 101a Chemical Biology
[ oc sn ]

Prerequisites: A satisfactory grade (C- or better) in BIOL 14a, BIOL 15b, and CHEM 25a and b, or the equivalent.

Explores how scientific work in chemistry led to fundamental understanding of and ability to manipulate biological processes. Emphasis is placed on chemical design and synthesis as well as biological evaluation and utility. Content based on scientific literature readings. Usually offered every second year.

CBIO 106b Chemical Biology: Medicinal Enzymology
[ sn ]

Prerequisites: Satisfactory grade in BIOL 14a, BIOL 15b, CHEM 25a and 25b, and BCHM 100a or the equivalent.

Introduces students to the conceptual framework and experimental methods in medicinal chemistry. Topics include mechanisms of drug-target interactions, strategies for lead optimization and issues in metabolism, pharmacokinetics and pharmacodynamics. Readings drawn from textbooks and the original scientific literature. Usually offered every second year.

CHEM 130a Advanced Organic Chemistry: Structure
[ sn ]

Prerequisite: A satisfactory grade in CHEM 25a and b, or the equivalent.

Chemical bonding and structure, stereochemical principles and conformational analysis, organic reaction mechanisms, structures and activities of reactive intermediates, and pericyclic reactions. Usually offered every year.

CHEM 132b Advanced Organic Chemistry: Spectroscopy
[ sn ]

Prerequisite: A satisfactory grade in CHEM 25a and b, or the equivalent.

Application of spectroscopy to the elucidation of structure and stereochemistry of organic compounds, with emphasis on modern NMR and MS methods. Usually offered every year.

CHEM 134b Advanced Organic Chemistry: Synthesis
[ sn ]

Prerequisite: A satisfactory grade in CHEM 25a and b, or the equivalent.

Modern synthetic methods are covered, with an emphasis on mechanism and stereochemical control. Discusses the formation of carbon-carbon single and double bonds and carbocycles and procedures for oxidation, reduction, and functional group interchange. Examines selected total syntheses. Usually offered every year.

CHEM 137b The Chemistry of Organic Natural Products
[ sn ]

Prerequisite: A satisfactory grade in CHEM 25a and b, or the equivalent.

Natural products chemistry is surveyed within a biosynthetic framework. Occurrence, isolation, structure elucidation, biosynthesis, and biomimetic synthesis are covered with an emphasis on modern methods of establishing biosynthesis and biomimetic syntheses. Usually offered every second year.

CHEM 146b Advanced Spectroscopy
[ sn ]

Prerequisites: A satisfactory grade in PHYS 10a,b, 11a,b, or 15a,b or the equivalent; MATH 10a,10b.

A detailed discussion of modern NMR methods will be presented. The course is designed so as to be accessible to non-specialists, but still provide a strong background in the theory and practice of modern NMR techniques. Topics include the theory of pulse and multidimensional NMR experiments, chemical shift, scalar and dipolar coupling, NOE, spin-operator formalism, heteronuclear and inverse-detection methods, Hartmann-Hahn and spin-locking experiments. Experimental considerations such as pulse sequence design, phase cycling, and gradient methods will be discussed. Guest lecturers will provide insight into particular topics such as solid-state NMR and NMR instrumental design. Usually offered every second year.

NBIO 136b Computational Neuroscience
[ dl sn ]

Prerequisites: MATH 10a or higher and one of the following: NBIO 140b/240b, PHYS 10b/11b/15b, BIOL 107a, or any COSI course.

An introduction to concepts and methods in computer modeling and analysis of neural systems. Topics include single and multicompartmental models of neurons, information representation and processing by populations of neurons, synaptic plasticity and models of learning, working memory, decision making and neural oscillations. The course will be based on in-class computer tutorials, assuming limited prior coding experience, with reading assignments and preparation as homework. Usually offered every second year.

PHYS 105a Biological Physics
[ sn ]

Physical forces in living matter are studied from the perspective offered by statistical mechanics, elasticity theory, and fluid dynamics. Quantitative models for biological structure and function are developed and used to analyze systems such as single molecule experiments, transcriptional regulation networks, the forces arising during DNA packaging in a virus, and mechanisms underlying mammalian pattern formation. Usually offered every second year.

QBIO 110a Numerical Modeling of Biological Systems
[ sn ]

Prerequisite: MATH 10a and b or equivalent.

Modern scientific computation applied to problems in molecular and cell biology. Covers techniques such as numerical integration of differential equations, molecular dynamics and Monte Carlo simulations. Applications range from enzymes and molecular motors to cells. Usually offered every second year.

QBIO 120b Quantitative Biology Instrumentation Laboratory
[ sn ]

Focuses on optical and other instruments commonly used in biomedical laboratories to make quantitative measurements in vivo and in vitro. Students disassemble and reconfigure modular instruments in laboratory exercises that critically evaluate instrument reliability and usability and investigate the origins of noise and systematic error in measurements. Usually offered every year.