University Bulletin 2002-03
Department of
Biochemistry

Courses of Study:
Major (B.A./B.S.)
Combined B.S./M.S.
Master of Science
Doctor of Philosophy

Department website: http://www.bio.brandeis.edu/index.shtml


Objectives

Undergraduate Major

The biochemistry major is designed to equip students with a broad understanding of the chemical and molecular events involved in biological processes. The biochemistry major provides a foundation for careers in medicine, biotechnology, or research in all branches of the biological sciences.

The general aim of the major is to ensure that the students first learn the necessary chemical and physical chemical background and then the basic principles and observations of biochemistry and molecular biology. The department also offers a variety of introductory and advanced courses in more specialized subjects such as neurobiology, X-ray crystallography, and physical biochemistry. These courses sample the range of subjects that can be studied by biochemical methods and from a biochemical point of view.

Graduate Program in Biochemistry

The graduate program in biochemistry leading to the degree of Doctor of Philosophy is designed to provide students with a deep understanding of the chemical principles governing the workings of biological macromolecules. The bioorganic chemistry track of this program gives students the option of training in organic chemistry in addition to biochemistry. The emphasis in the graduate program is placed upon experimental research work to train students to carry out independent original research. However, students are required to complete formal course work in advanced biochemistry and physical biochemistry. Students in the bioorganic chemistry track supplement this core curriculum with courses in organic synthesis and other topics in organic chemistry. Additional courses and seminars are available in a wide range of subjects, including enzyme regulation and mechanism, neurobiology, immunology, structural biochemistry, membrane biology, and molecular genetics. Students are encouraged to choose advanced courses and seminars according to their particular interests. Doctoral research topics are chosen in areas under investigation by the faculty; these include problems in macromolecular structure and function, enzyme function and regulation, RNA processing, gene regulation, membrane transport and receptor function, molecular pharmacology, mechanisms of cell motility, microbial metabolism, and the biochemistry of cellular electrical excitability. A theme running through this research is the relationship of biochemical functions to underlying molecular structures and mechanisms.

The graduate program in biochemistry leading to the degree of Master of Science is designed to give students a substantial understanding of the chemical and molecular events in biological processes and experience in research. The program is divided among formal course work, biochemical techniques, and a research project. Additional courses and seminars are available in a wide range of subjects, as described above.


How to Become an Undergraduate Major


Students who are interested in majoring in biochemistry should speak with the department advising head.


How to Be Admitted to the Graduate Program


The general requirements for admission to the Graduate School, given in an earlier section of the Bulletin, apply here. Applicants for admission to the biochemistry Ph.D. program are also required to take the Graduate Record Examination. It is strongly suggested that the applicant take one of the advanced sections of this examination. The applicant's undergraduate curriculum should include fundamental courses in biology and chemistry.


Faculty


Daniel Oprian, Chair
Structure-function studies of visual pigments and other cell surface receptors.

Jeff Gelles
Mechanisms of mechanoenzymes. Stochastic processes in single enzyme molecules. Light microscopy as a tool to study enzyme mechanisms.

Ulrich Genick
Structural investigation of signaling in the phytochrome system.

Nikolaus Grigorieff
High resolution electron cryo-microscopy of membrane proteins and channels.

Lizbeth Hedstrom
Enzyme structure-function studies. Protein engineering. Design of enzyme inhibitors.

Dorothee Kern
Dynamics of enzymes. Magnetic resonance methods.

John Lowenstein
Role of phospholipids in hormone action. Regulation of lipogenesis. Regulation and function of the purine nucleotide cycle. Regulation and function of adenosine production in the heart. Techniques of cloning and high level expression of proteins.

Christopher Miller
Structure and function of ion channel proteins. Membrane transport and mechanisms of electrical excitation.

Melissa Moore, Undergraduate Advising Head
Molecular biology of self-splicing introns and the splicesome. Mechanisms of RNA catalysis.

Gregory Petsko (Director, Rosenstiel Center)
X-ray crystallographic analysis of protein structure and enzyme mechanisms.

Dagmar Ringe (Rosenstiel Center)
Structures of enzymes and enzyme-substrate complexes. X-ray crystallography.


Requirements for the Undergraduate Major


Degree of Bachelor of Arts

One year of general chemistry with laboratory; one year of organic chemistry with laboratory; one year of physics taught using calculus (PHYS 11a,b or 15a,b) with laboratory; BIOL 22a-formerly BIBC 22a with laboratory (Genetics and Molecular Biology); BIOL 22b with laboratory (Cell Structure and Function) (the above courses must be taken prior to the senior year); BCHM 100a (Introductory Biochemistry); one year of physical chemistry, CHEM 41a (Physical Chemistry, Lectures I) and either BCHM 104b (Physical Chemistry of Macromolecules) or CHEM 41b (Physical Chemistry, Lectures II); and one elective from any 100-level course (excluding research courses) offered in the biochemistry and biology departments. With advance approval from the biochemistry department advising head, an upper-level course offered by another department (e.g., chemistry or physics) may also fulfill the elective requirement. The laboratory associated with CHEM 41a is optional.

Degree of Bachelor of Science

In addition to the degree requirements listed above for the Bachelor of Arts degree, the Bachelor of Science degree requires one year of BCHM 101a and b (Advanced Biochemistry).

Required of all students: No course offered for major requirements may be taken pass/fail. Grades below C- in upper-level courses (CHEM 41a and b, and any course numbered 100 or above) cannot be used to fulfill the requirements for the major. Furthermore, no more than one D will be allowed in any other course required for the major.

Senior Honors Program

In addition to the degree requirements listed above, departmental honors require completion of two semesters of BCHM 99 (Research for Undergraduates), submission of an acceptable research thesis, and a final grade point average of 3.00 or better in the sciences and mathematics. Honors candidates are also expected to give a short oral presentation of their thesis research to members of the department at the end of their senior year. BCHM 99 may not exceed three semester credits. Petition to the department for participation in this program is made at the beginning of the senior year.


Combined B.S./M.S. Program


In addition to all courses requires for the Bachelor of Science degree, the B.S./M.S. degree required completion of one additional elective (excluding research courses) approved in advance by the biochemistry department advising head, three semesters of research (one or two semesters of BCHM 99 plus one or two semesters of BCHM 150), a full-time (i.e., no concurrent coursework) summer research residency lasting at least 10 weeks, submission of an acceptable thesis, a GPA of 3.00 or better in the sciences and mathematics, and grades of B- or better in all 100-level biochemistry and biology courses. This program requires completion of 38 courses; no more than four semesters of research (BCHM 99 or 150) can count toward this total. Application to this program is made to the department and Graduate School no later than May 1 preceding the senior year, and all work, including the thesis, must be completed by the time the B.S. is awarded. To qualify for the B.S./M.S. degree, the thesis must constitute a significant research contribution; if a thesis is found unacceptable under B.S./M.S program, it will automatically be considered under the Honors program.

In order to complete the Honors Program or the combined B.S./M.S. Program, it is advisable to gain exemption where possible from introductory courses in science and mathematics. This is especially important for the premedical students who must also fulfill the requirements imposed by medical schools.


Requirements for the Degree of Master of Science


Program of Study

Students must successfully complete an approved program of at least six courses. These courses are:

BCHM 101a Advanced Biochemistry: Enzyme Mechanisms

BCHM 101b Advanced Biochemistry: Information Transfer Mechanisms

BCHM 102a Quantitative Approaches to Biochemical Systems

BCHM 104b Physical Chemistry of Macromolecules

BCHM 200a,b Biochemical Techniques (Lab rotations)

Residence Requirement

The minimum residence requirement is one year.

Language Requirement

There is no language requirement.

Thesis

The student must complete an acceptable M.S. thesis describing original research.


Requirements for the Degree of Doctor of Philosophy


Program of Study: Biochemistry Ph.D.

Students must successfully complete the curriculum defined below.

A. The core curriculum consisting of:

BCHM 101a ? Advanced Biochemistry: Enzyme Mechanisms

BCHM 101b Advanced Biochemistry: Information Transfer Mechanisms

BCHM 102a? Quantitative Approaches to Biochemical Systems

BCHM 104b Physical Chemistry of Macromolecules

BCHM 200a,b Biochemical Techniques (Lab rotations)

CONT 300b Ethical Practices in Health-Related Sciences

B. An advanced elective course (number between 100 and 199) from the Biochemistry, Biophysics and Structural Biology, Chemistry, Molecular and Cell Biology, or Neuroscience Programs. Other advanced courses can be substituted with approval of the Chair.C. Three seminar courses selected from courses numbered BCHM 219 to 250. Other advanced courses can be substituted with approval of the Chair.

Students will typically complete the core curriculum in the first year and complete the remaining requirements in subsequent years in the program.

Program of Study: Bioorganic Chemistry Track

In order to receive a Ph.D. in biochemistry with a specialization in bioorganic chemistry, students must complete:

A. The core curriculum defined above.

B. CHEM 134a Advanced Organic Chemistry: SynthesisC. One other advanced chemistry course, chosen from the following:

CHEM 111a Computational Chemistry

CHEM 130a Advanced Organic Chemistry: Structure

CHEM 131a Advanced Organic Chemistry: Topics in Structure and Reactivity

CHEM 132b Advanced Organic Chemistry: Spectroscopy

CHEM 137b The Chemistry of Organic Natural Products

CHEM 229b Introduction to X-Ray Structure Determination

CHEM 235b Advanced NMR Spectroscopy

D. Two seminar courses selected from courses numbered BCHM 219 to 250. Other advanced courses can be substituted with approval of the Chair.

Students typically complete the core curriculum in the first year and complete the remaining requirements in subsequent years in the program. However bioorganic track students have the option of replacing BCHM 102a or BCHM 104b with CHEM 134a in the first year and completing the replaced course in the second year.

Teaching Requirement

As a part of their Ph.D. training, students are required to assist with the teaching of two, one-semester courses.

Residence Requirement

The minimum residence requirement is three years.

Language Requirements

There is no foreign language requirement.

Financial Support

Students may receive financial support (tuition and stipend) throughout their participation in the Ph.D. program. This support is provided by a combination of University funds, training grants, and individual research grants.

Qualifying Examinations

An oral qualifying examination must be taken following the first year of course work. In this examination, the student will be asked to present two propositions. The subject of one proposition will be assigned and the other will be an original proposition put forth by the student. In addition the student must successfully pass a comprehensive examination administered following the second year of course work.

Dissertation and Defense

A dissertation will be required that summarizes the results of an original investigation of an approved subject and demonstrates the competence of the candidate in independent research. This dissertation will be presented in a departmental lecture and defended in a Final Oral Examination.


Courses of Instruction



(1-99) Primarily for Undergraduate Students


BCSC 1a Designer Genes
[ sn ]
Does NOT satisfy the requirement for the major in biochemistry.
Enrollment limited to 20.
We are living during a far-reaching biological revolution. Information stored in genes as DNA, the hereditary material of life, conversion of this information into proteins. Identifying undesirable mutations. Creating desirable mutations. Cloning of cells, organs, and animals in agriculture and medicine. Present and future applications. Usually offered every second year. Will be offered in the fall of 2002.
Mr. Lowenstein

BCHM 98a Readings in Biochemistry
Prerequisites: BIOL 22a (formerly BIBC 22a); BCHM 100a; and one year of organic chemistry with laboratory. Enrollment limited. Signatures of the major advisor and mentor required. Does NOT satisfy the requirement for the major in biochemistry.
Directed scholarship on selected topics in biochemistry for outstanding juniors or seniors. Regularly scheduled discussion and written assignments leading to a substantive term paper. The tutorial is arranged only by mutual agreement between a faculty mentor and student. Usually offered every year. Will be offered in the fall of 2002.
Staff

BCHM 99a Research for Undergraduates
Prerequisites: BIOL 22a (formerly BIBC 22a); and BCHM 100a; one year of organic chemistry with laboratory. Requirement of BCHM 100a may be waived. Enrollment limited. Signature of department chair required.
Undergraduate research. A maximum of three course credits may be taken as BCHM 99a and/or 99b. At the discretion of the department, one semester may be taken for double credit (99e). Offered every year. Will be offered in the fall of 2002.
Staff

BCHM 99b Research for Undergraduates
See BCHM 99a for special notes and course description. Offered every year.
Staff

BCHM 99e Research for Undergraduates
See BCHM 99a for special notes and course description. Offered every year. Will be offered in the fall of 2002.
Staff


(100-199) For Both Undergraduate and Graduate Students


BCHM 100a Introductory Biochemistry
[ qr sn ]
Prerequisite: One year of organic chemistry with laboratory. Enrollment limited to 70.
Topics include chemistry, reaction, and metabolism of biologically important compounds; formation and utilization of "energy-rich" compounds; introduction to enzyme mechanisms; interrelation and comparison of basic biochemical and chemical processes; and metabolic regulation. Usually offered every year in multiple sections. Will be offered in the fall of 2002.
Ms. Hedstrom (fall), Mr. Lowenstein (fall), Mr. Grigorieff (spring)

BCHM 101a Advanced Biochemistry: Enzyme Mechanisms
[ sn ]
Prerequisites: One year of organic chemistry with laboratory and
BCHM 100a, or their equivalent. Enrollment limited to 50.
Describes the principles of biological catalysts and the chemical logic of metabolic pathways. Representative enzymes from each reaction class are discussed 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. Will be offered in the fall of 2002.
Ms. Kern and Mr. Oprian (fall)

BCHM 101b Advanced Biochemistry: Information Transfer Mechanisms
[ sn ]
Prerequisites: One year of organic chemistry with laboratory and
BCHM 100a, or their equivalent. Enrollment limited to 50.
Addresses fundamental issues of gene expression and signal transduction at a molecular level. Discusses parallels between nucleic acid and protein biosynthesis, modification, transport, and degradation with an emphasis on understanding the mechanisms of specificity and regulation of these complex macromolecular processes. Usually offered every year. Will be offered in the spring of 2003.
Ms. Moore and Mr. Oprian

BCHM 102a Quantitative Approaches to Biochemical Systems
[ sn ]
Prerequisites: PHYS 11a, b and BCHM 100, or their equivalent. Enrollment limited to 50.
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. The physical bases of spectroscopic and diffraction methods commonly used in the study of proteins and nucleic acids will also be discussed. Usually offered every year. Will be offered in the fall of 2002.
Mr. Gelles

BCHM 104b Physical Chemistry of Macromolecules
[ sn ]
Prerequisite: CHEM 41a or equivalent and BCHM 100a or equivalent. Enrollment limited to 50.
Illustrates the basic principles on which biological macromolecules are constructed and by which they function. Overall structures of proteins, nucleic acids, and membranes are described 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. Usually offered every year. Will be offered in the spring of 2003.
Mr. Miller

BCHM 150a Research for B.S./M.S. Candidates
[ sn ]
Prerequisites: BIOL 22a (formerly BIBC 22a) and BCHM 100a; one year of organic chemistry and laboratory; BCHM 99d. Enrollment limited and signature of the advising head required.
The final semester(s) of laboratory research under the B.S./M.S. Program, to be pursued under the supervision of a faculty advisor. Usually offered every year. Will be offered in the fall of 2002.
Ms. Moore and Staff

BCHM 150b Research for the B.S./M.S. Candidates
[ sn ]
See BCHM 150a for special notes and course description. Usually offered every year. Will be offered in the spring of 2003.
Ms. Moore and Staff

BCHM 151b Ion Channel Proteins
[ sn ]
This course considers the molecular properties of ion channels, the most basic element of molecular hardware in the nervous system. Examines the molecular architecture of channels and the mechanisms of channel activity. The mechanisms of voltage-dependence, ion selectivity, and channel gating will be emphasized. Usually offered every fourth year. Last offered in the spring of 1998.
Mr. Miller

BCHM 170b Bioinformatics
[ sn ]
Prerequisites: Familiarity with computing is necessary and a basic biochemistry course is recommended. A joint offering between Brandeis University and Wellesley College. The course will meet on the Wellesley campus and bus service will be provided. Enrollment limited to 15 students each from Brandeis and Wellesley.
Familiarizes students with the basic tools of bioinformatics and provides a practical guide to biological sequence analysis. Topics covered include an introduction to probability and statistics; sequence alignments; database searches; alignments and phylogenetic trees; sequence pattern discovery; structure determination by secondary structure prediction; and three dimensional structure prediction by homology modeling. In all cases the strengths and limitations of the methods will be discussed. Usually offered every second year. Last offered in the spring of 2002.
Mr. Cohen, Ms. Ringe (Brandeis), and Mr. Webb (Wellesley)

BCHM 171b Protein X-Ray Crystallography
[ sn ]
Prerequisites: Familiarity with computing is necessary and a basic biochemistry course is recommended.
A practical guide to the determination of three dimensional structures of proteins and nucleic acids by X-ray diffraction. Students will learn theory behind diffraction from macromolecular crystals and will carry out all of the calculations necessary to solve a protein structure at high resolution. Usually offered every fourth year. Last offered in the fall of 1997.
Mr. Petsko and Ms. Ringe


(200 and above) Primarily for Graduate Students


BCHM 200a and b Biochemistry Techniques
Prerequisite: BCHM 101. May be taken concurrently. Limited enrollment.
Usually offered every year.
Mr. Gelles and Staff


Advanced Topic Courses

Topics are repeated usually at two- to three-year intervals.

BCHM 219b Enzyme Mechanisms
Ms. Hedstrom

BCHM 220a Proteases
Ms. Hedstrom

BCHM 222a Protein Kinases and Phosphatases
Mr. Lowenstein

BCHM 223a Signal Transduction
Mr. Oprian

BCHM 224a Single-Molecule Biochemistry and Biophysics
Mr. Gelles

BIBC 224b The RNA World
Prerequisites: BCHM 100a, BIOL 105b (formerly BIBC 105b), or permission of the instructor.
This course employs seminars and lectures to approach a wide range of topics in RNA research. Topics include RNA enzymes, RNA structure, protein-RNA interactions, pre-MRNA splicing, and RNA localization. Usually offered every year.
Ms. Moore

BCHM 271a Protein X-Ray Crystallography, Part 2
Prerequisite: BCHM 271b.
A continuation of BCHM 271b. Offering dependent on BCHM 271a class interest.
Mr. Petsko

BCHM 271b Protein Crystallography
Prerequisite: CHEM 229b.
A practical guide to the determination of three-dimensional structures of proteins and nucleic acids by X-ray diffraction. Students learn the theory behind diffraction from macromolecular crystals and carry out all the calculations necessary to solve a protein structure at high resolution. Usually offered every second year. Last offered the fall of 2000.
Mr. Petsko


Graduate Research

BCHM 401d Biochemical Research Problems
Independent research for the M.S. and Ph.D. degrees. Specific sections for individual faculty members as requested. Will be offered in the fall of 2003.
Staff


Journal Club, Colloquia, and Research Clubs

In addition to the formal courses announced above, all graduate students are expected to participate in the department's Research Clubs and Colloquia. Colloquia are general meetings of the department in which department and guest speakers present their current investigations. Research clubs are organized by various research groups of the department.


CONT 300b Ethical Practice in Health-Related Sciences
Required of all first-year graduate students in health-related science programs. Not for credit.
Scientists are becoming increasingly aware of the importance of addressing ethical issues and values associated with scientific research. This course, taught by University faculty from several graduate disciplines, will cover major ethical issues germane to the broader scientific enterprise, including areas or applications from a number of fields of study. Lectures and relevant case studies will be complemented by two public lectures during the course. Usually offered every year.
Mr. Fulton


Cross-Listed Courses


CHEM 235b
Advanced NMR Spectroscopy