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Chemistry: Course 5

Undergraduates have the opportunity to participate in a variety of research areas. A partial list of available research topics and faculty advisors appears below. Students may consult with the Coordinator for more detailed information and are encouraged to speak directly with faculty supervisors.

Instruction forms on procedures for registering for 5.UR and 5.URG are available from the Chemistry Education Office (2-204). Credit is obtained for undergraduate research by registering for course 5.UR or 5.URG and by submitting a for credit UROP application before the UROP office deadlines. To receive credit, students enrolled in 5.UR (research for Pass/Fail grade) must file a Progress Report with the UROP coordinator. Subject 5.URG (research for Letter Grade) is open to juniors and seniors for 9 or 12 units per semester. To receive credit, students are required to submit a ten-page final written report to their research advisor prior to the last day of classes.

All new UROP students in the Department of Chemistry must complete the Training Needs Assessment form which is accessible through the EH&S Office's training web site. An MIT Certificate is required along with a Kerberos username and MIT I.D. the above address will bring you to the EH&S Office's home page. Follow the link to EH&S training. Verify that the user information is correct and complete the Training Needs Assessment Form. This will provide a list of training requirements and information on how to complete them. Virtually all researchers (with the exception of some theoretical chemists) will be required at a minimum, to complete the following steps prior to begining work in areas where hazardous chemicals are in use. Even if you do not work in areas where hazardous chemicals are in use, you will still need to complete step 5, listed below.

  1. Attend the Chemical Hygiene and Safety Lecture presented in January or view a DVD copy of the lecture. Copies of the lecture can be borrowed from Chemistry Headquarters in room 18-393.

  2. Read and understand the Chemistry Department Chemical Hygiene Plan and Safety Manual. Copies of the book can be obtained in Chemistry Headquarters in room 18-393.

  3. Receive Initial Lab Specific Chemical Hygiene Plan and Safety Training from your Laboratory Supervisor or their designee (you will need to obtain the laboratory Supervisor's signature on the EH&S Clearance form).

  4. Complete the training course, Managing Hazardous Waste. This is offered as a web based course and is accessible through the EH&S office's training website mentioned above. this is an annual requirement. As the expiration date approaches, an automatic e-mail reminder will be sent to indicate that you must log on to the training website and complete the web course again.

  5. Obtain the EH&S Clearance form from Chemistry Headquarters in 18-393. New UROP students must sign the EHS Clearance Form and submit it to Chemistry Headquarters, indicating that all training requirements stated on the form have been met. In the case that work will not be performed with hazardous substances or in areas where hazardous substances are in use, the laboratory supervisormust sign the form. Please contact Jim Doughty EH&S Coordinator (324-6132, jdoughty@mit.edu) with any questions.


Prof. Moungi Bawendi, 6-221, x3-9796, mgb@mit.edu
Bawendi Group Homepage
Science and application of semiconductor and magnetic nanocrystals. Synthesis, characterization, spectroscopy, applications to opto-electronic devices including photodetectors, photovoltaics and light emission, and applications in biological and biomedical imaging.
 
Prof. Stephen L. Buchwald, 18-490, x3-1885, sbuchwal@mit.edu
Buchwald Group Homepage
Organic synthesis based on organotransition metal technology, mechanisms of organometallic reactions, main group and transition metal organometallic chemistry.
 
Prof. Sylvia T. Ceyer, 6-217, x3-4537, stceyer@mit.edu
Ceyer Group Homepage
Experimental studies of the dynamics of the interactions of molecules with solid surfaces, including investigations of mechanisms of heterogeneous catalysis and etching reactions.

Prof. Christopher C. Cummins, 6-435, x3-5332, ccummins@mit.edu
Cummins Group Homepage
Inorganic radical chemistry. Activation of small molecules including dinitrogen and the nitrogen oxides. Development of new synthetic methods for inorganic chemistry.
 
Prof. Rick L. Danheiser, 18-298, x3-1842, danheisr@mit.edu
Danheiser Group Homepage
Development of new methods for the synthesis of organic compounds; applications to synthesis of biologically important compounds. Green chemistry, including the development of environmentally friendly methods for chemical synthesis.

Prof. Catherine L. Drennan, 16-573A, x3-5622, cdrennan@mit.edu
Drennan Group Homepage
Structure and function studies of metalloenzymes that are medically important or involved in environmental remediation

Prof. John M. Essigmann, 56-669B, x3-6227, jessig@mit.edu,
Essigmann Group Home Page
Biochemical and molecular mechanisms of cancer induction by chemicals and radiation; mechanisms for DNA repair; and design of novel anti-tumor agents that hijack transcription factors.

Prof. Robert W. Field, 6-219, 3-1489, rwfield@mit.edu, Field Group Page
Multiple resonance laser spectroscopy of small molecules in pulsed supersonic molecular beams using a variety of cw, nanosecond, and femtosecond lasers, in combination with both cw and chirped-pulse millimeter-wave sources. Projects include construction of sources of transient molecules, optimization of signal detection devices, generation of software for laser- scan control, data acquisition, spectrum calibration, and development of unconventional models to fit frequency-domain spectra and to visualize the dynamical mechanisms encoded in these spectra.

Prof. Gregory C. Fu, 18-290, x3-2664, gcf@mit.edu
Fu Group Homepage
Development of new reagents and methods for organic chemistry, with an emphasis on asymmetric catalysis, and elucidation of reaction mechanisms.
 
Prof. Robert G. Griffin, NW14-322, x3-5597, griffin@ccnmr.mit.edu
Nuclear magnetic resonance in solids, applications of NMR to biological problems, high field dynamic nuclear polarization and pulsed EPR.
 
Prof. Barbara Imperiali, 18-590, x3-1838, imper@mit.edu
Imperiali Group
Protein structure, function, and design. Multidisciplinary approach employs synthesis, spectroscopy, molecular modeling, enzymology and molecular biology to address fundamental problems at the interface of chemistry and biology.
 
Prof. Timothy F. Jamison, 18-492, x3-2135, tfj@mit.edu
Jamison Group Homepage
Organic Chemistry. Development of new organic reactions and their use in the synthesis of natural products and related molecules.
 
Prof. Alexander M. Klibanov, 56-579, x3-3556, klibanov@mit.edu
Enzymes as catalysts in organic chemistry, enzymatic catalysts in non-aqueous media, microbicidal materials, delivery of pharmaceutical proteins and nucleic acids.

Prof. Stuart Licht, 16-573B, 452-3525, lichts@mit.edu
Licht Group Homepage
Mechanistic studies of enzymes and ion channels. One area of interest is how enzymes and ion channels may use ATP hydrolysis as an energy source to carry out conformational changes that would otherwise be energetically disfavored. Another general area of interest is investigating how protein-protein interactions affect protein function. For example, under some circumstances, the opening of one ion channel can influence the probability that a neighboring ion channel will open. Similarly, when the product of an enzymatic reaction affects the activity of an ion channel (or another enzyme), physical association between the two proteins may link the proteins functionally by producing a high effective concentration of that product near its binding site. A third area of interest is engineering metal binding sites into ion channels as a tool for studying ion channel gating and bioinorganic reactivity at the single-molecule level.

Prof. Stephen J. Lippard, 18-498, 3-1892, lippard@mit.edu,
Lippard Group Home Page
Platinum anticancer drugs; synthetic chemistry related to diiron metalloenzymes; structural and mechanistic studies of bacterial monooxygenases, including soluble methane monooxygenase; metalloneurochemistry, including mobile zinc and nitric oxide in the brain; nitric oxide chemistry of zinc and iron thiolates and clusters.

Prof. Mohammad Movassaghi, 18-292, x3-3986, movassag@mit.edu
Movassaghi Group Homepage
Complex natural product total synthesis. Discovery, development, and mechanistic studies of new reactions for organic synthesis.

Prof. Keith A. Nelson, 6-235, x3-1423, kanelson@mit.edu
Nelson Group Homepage
Picosecond and femtosecond laser spectroscopy of phase transitions, liquid-glass transitions, chemical reactions, and other condensed matter phenomena; thin film characterization; nonlinear interactions of light with condensed matter; optical control over material behavior.

Prof. Sarah E. O’Connor, 18-592, 324-0180, soc@mit.edu
O’Connor Group Homepage
The O’Connor group studies natural product biosynthesis. We use nature’s biosynthetic pathways to make complex molecules.

Prof. Jonas C. Peters, 18-296, 3-1819, jcpeters@mit.edu
Peters Group Home Page: http://web.mit.edu/petersgroup/ inorganic/ organometallic synthesis, small molecule activation, redox reactions, catalytic energy conversion

Prof. Richard Schrock, 6-331, x3-1596, rrs@mit.edu, Schrock Group
Schrock Group Homepage
Organometallic synthesis, mechanisms, homogeneous catalysis, olefin metathesis, reduction of dinitrogen, new polymers, asymmetric olefin metathesis, living polymerization of olefins.

Prof. Robert J. Silbey, 6-129, x3-1470, silbey@mit.edu
Quantum and statistical mechanics especially applied to relaxation processes in molecules and condensed phases. (Completion of 5.61 and 5.62 desirable.)

Prof. Joanne Stubbe, 18-598, x3-1814, stubbe@mit.edu,
Mechanisms and structure of enzymatic reactions including ribonucleotide reductases, purine biosynthetic pathway enzymes, enzymes involved in DNA repair and enzymes involved in making biodegradable polyesters and rubber; structure and mechanisms of DNA cleavers such as bleomycins, natural products used clinically in the treatment of cancer; design of mechanism based inhibitors as tools to study mechanism and as potential cancer, antiviral and antibacterial therapeutics; use of molecular biological methods including site directed mutagenesis, use of rapid kinetics methods including stopped flow and rapid freeze quench to study intermediates in reactions; use of yeast as a model system to investigate iron homeostasis and how metallo-cofactors of proteins are generated in vivo; use of yeast as a model system to study DNA replication and repair by modulation of deoxynucleotide pools.
 
Prof. Timothy M. Swager, 18-398,x3-1801, tswager@mit.edu,
Swager Group Home Page Supramolecular and materials chemistry with an emphasis on the synthesis and construction of functional assemblies. Since chemosensors require recognition elements to discriminate chemical signals, molecular recognition pervades the research. Also, integration of molecular recognition principles in the design of supramolecular catalysts provide unique specificity and mimic the characteristics of enzymes. In the area of liquid crystals, molecular complementary and receptor-ligand interactions provide novel organizations.
 
Prof. Steven R. Tannenbaum, 56-731A, x3-3729, srt@mit.edu
Tannenbaum Group Homepage
Applications of chromatography, mass spectrometry, and affinity methods for identification, detection, and analysis of biological molecules. Applications include inflammation (nitric oxide), liver function and toxicology, proteomics, metabolomics, drug development.

Prof. Alice Y. Ting, 18-496, 452-2021, ating@mit.edu
Ting Group Home Page
Design and synthesis of new molecules for probing signal transduction in living cells. Fluorescent reporters for protein trafficking, enzyme activity, post-translational modifications, receptor recycling, and protein-protein interactions. Directed evolution of new ligases for site-specific labeling of recombinant proteins in living cells. Improved quantum dots for single-molecule imaging of proteins in living cells.
 
Prof. Andrei Tokmakoff, 6-225, x3-4503, tokmakof@mit.edu
Tokmakoff Group Home Page
Development and use of time-resolved spectroscopy for studies of chemical and biological dynamics. Design of experiments to study transient structure and confirmation of proteins, peptides, and other molecules in solution. Protein folding and unfolding kinetics; protein dimerization and aggregation. Synthesis of isotope-edited peptides for spectroscopic studies of folding. Hydrogen bond network rearrangements in water. Proton transfer mechanisms in water. Study of proton transfer mediated by hydrogen bonds. Collective structure and structural change of liquids. Development and use of two-dimensional vibrational spectroscopy.

Prof. Troy Van Voorhis, 6-229, x3-1488, tvan@mit.edu
Van Voorhis Group Homepage
Electronic structure theory of molecules. Investigation of the mechanisms and dynamics of electron transfer reactions. Accurate description of excited state chemistry.
MIT
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77 Massachusetts Avenue, Bldg. 7-104, Cambridge, MA 02139
Tel: 617-253-7306, Fax: 617-258-8816

UROP Contacts


UROP Coordinator:

Prof. Christopher Cummins
6-435, x3-5332
ccummins@mit.edu

UROP Contact

Melinda Cerny
Chemistry Education Office
2-204, x3-0909
cerny@mit.edu

Department Head:

Prof. Timothy Swager
18-398, x3-1801
tswager@mit.edu

UROP Payroll:

Fionnuala Coary
18-394, x3-1808,
fcoary@mit.edu

UROP for Credit:

P/D/F: 5.UR
Letter Grade: 5.URG (Jr/Sr only)