Current Research

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 (6-205). Credit is obtained for undergraduate research by registering for course 5.UR or 5.URG and by submitting a for credit UROP application before theUROP 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, not to exceed a cumulative total of 24 units.  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.

Safety

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 ID 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 beginning 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) New personnel must attend the Chemical Hygiene and Safety Lecture presented in January or view a video recording of the lecture. The video is accessible through the training web site listed above.

(2) Read and understand the Chemistry Department Chemical Hygiene Plan and Safety Manual. Copies of the book can be obtained in Chemistry Headquarters or from Scott Ide (4-469).

(3) Receive Initial Lab Specific Chemical Hygiene and Safety Training from your Laboratory Supervisor or their EH&S Representative. This is an orientation to the location of safety equipment in your laboratory and to special hazards associated with the research in your group.

(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 listed above. This is an annual requirement.

(5) Obtain the EH&S Clearance Form from Chemistry Headquarters or from Scott Ide (4-469). New members of the Department must sign the EHS Clearance Form and obtain their supervisor’s signature and submit it to Scott Ide (4-469). You must still submit the form if you will not be working in an area where hazardous materials are in use. No individual is permitted to work in areas in which chemicals are in use until all of the above steps have been completed and a signed EHS Clearance Form is submitted.

Note: Additional training is required for individuals working with other hazardous materials including (but not limited to) lasers, radioactive materials, and certain biohazardous materials. Completing the Training Needs Assessment Form will dictate your training needs. It is the responsibility of the researcher to ensure that all of these training requirements are met.

Faculty Research Descriptions

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 and transition metal organometallic chemistry.

Prof. Arup Chakraborty, E19-502c, x3-3890, arupc@mit.edu,

See the Chakraborty lab website for information on current research projects.

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. Mircea Dinca, 2-227, x3-4154, mdinca@mit.edu, Dinca Research Group

Functional Inorganic Chemistry. Synthesis and characterization of microporous materials and other extended solids. Applications in electronically conductive materials, light harvesting, and microporous thin film/nanoparticle research.

Prof. Catherine L. Drennan, 68-680, 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 nanosecond pulsed tunable lasers, in combination with chirped-pulse millimeter-wave sources. Projects include construction of sources of transient molecules, assembly of a molecular beam vacuum system, optimization of signal detection devices, generation of software for advanced pattern recognition, data acquisition, spectrum calibration, and development of unconventional effective Hamiltonian and Quantum Defect models to fit frequency-domain spectra and to visualize the dynamical mechanisms encoded in these spectra.

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 for batch and continuous flow synthesis of natural products and related molecules.

Prof. Jeremiah Johnson, 18-296, x3-1819, jaj2109@mit.edu, The Johnson Research Group

We use the tools polymer and synthetic organic chemistry to design and synthesize new polymer materials for biological and energy applications.

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. 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

Our research group’s interest is complex natural product total synthesis. An integral part of our research is the discovery, development, and mechanistic studies of new reactions for organic synthesis. These endeavors enable expeditious and practical access to architecturally complex, and in many cases, potently bioactive molecules. Applicants with a particularly strong background in theoretical and experimental organic chemistry are welcome to contact us.

Additionally, a unique opportunity currently exists for an individual with strong analytical, organizational, and communication skills interested in a cheminformatics project involving complex bioactive molecules. The project involves a multi-stage development and management of a visualization platform for large data sets related to screening results of our molecular libraries conducted at National Institutes of Health and elsewhere.

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. Elizabeth M. Nolan, 16-573B, x2-2495, lnolan@mit.edu, The Nolan Group

Bioinorganic chemistry, metalloenzymology, antimicrobial peptides/proteins and small molecules, chemistry of the innate immune system.

Prof. Bradley Pentelute, 16-573A, x4-0180 blp@mit.edu, Pentelute Group

Multidisciplinary group that uses chemistry to probe anthrax toxin and mirror image proteins.

Prof. Matthew Shoulders, 18-598, x2-3525, mshoulde@mit.edu

Maintaining the proper three-dimensional structure, concentration, activity, and localization of proteins is a fundamental challenge for all organisms. The cellular protein homeostasis network regulates protein synthesis, folding, post-translational modifications, secretion, and degradation. Dysregulated proteostasis is inextricably linked to disease states. The cell has, therefore, evolved sophisticated stress-responsive signaling pathways to resolve proteostatic imbalance. The ubiquity of the proteostasis network in cells suggests regulating the cellular mechanisms underlying protein folding, post-translational modifications, secretion, and degradation as a promising paradigm for treating broad swaths of disease. We employ a multi-disciplinary approach to (1) understand how the cell remodels itself to address challenges to proteostasis, (2) elucidate the pathophysiology of protein folding-related diseases with poorly defined etiology, and (3) target the biological processes we uncover for the development of first-in-class small molecule drugs. We study the proteostasis network in the endoplasmic reticulum (ER), a subcellular compartment responsible for folding and processing ~1/3 of the eukaryotic proteome—including secreted, membrane, and lysosomal proteins. A portion of our research program leverages new chemical biology tools to elucidate the fundamental mechanisms of how cells respond to dysregulated proteostasis, with a focus on cancer-related and stress-induced post-translational protein modifications. We also work to understand the pathology of and develop therapeutic strategies for rare and orphan diseases originating in missense mutations to extracellular matrix proteins.

Prof. Joanne Stubbe,18-598, x3-1814, stubbe@mit.edu, The Stubbe Group

I.Understanding the mechanism and structures of enzymes involved in nucleic acid metabolism. Use of chemistry and biology to study the mechanism of catalysis of radical based reactions in biology including ribonucleotide reductases. These enzymes provide the monomeric precursors required for DNA replication and repair. This information is used to rationally design effective therapeutics. Gemzar is a drug used clinically in the treatment of non small cell lung carcinoma and pancreatic cancer that was designed to specifically inhibit ribonucleotide reductases. Methods include, rapid kinetics (stopped flow and Vis spectroscopy, rapid freeze quench EPR spectroscopy, site specific incorporation of unnatural amino acids, use of fluorescent probes to study dynamics of enzymes in vitro and in vivo. II. Metabolic engineering of biodegradable polymers with properties of thermoplastics. Investigation of the synthases that make polyoxoesters in vivo and in vitro using physical organic and synthetic chemistry, fluorescent labeling in vivo, cryo electron microscopy and tomography. The long range goal is to replace the oil based polymers that are non biodegradable and the major ingedient of plastic trash with thes biodegradable polymers expressed in heterologous systems (bacteria or plants)

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.