Wellesley College Biological Chemistry Faculty

Faculty

allen&student michelle&prof

The Biological Chemistry major includes faculty and courses from both the Biological Sciences and Chemistry Departments. Any member of these two departments may serve as research mentors for majors. In the last five years (2001-2006) the following faculty have served as advisors for independent and thesis research for Biological Chemistry majors. Each faculty member is represented by a structure involved in his or her research.

		Mary Allen, Biological Sciences Personal website C-phycocyanin (Neild, J.; Rizkallah, P. J.; Barber, J.; Chayen, N. E. 2003. The 1.45 Å three-dimensional structure of C-phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus. J. Struct. Biol. 141, 149-155.) The crystal structure of c-phycocyanin from the cyanobacterium S. elongatus. Students in the Allen lab have performed many studies on c-phycocyanin, the major light harvesting pigment and nitrogen storage molecule in cyanobacteria, and related molecules that are central to cyanobacterial physiology and biochemistry.

		Chris Arumainayagam, Chemistry Personal website Tetrahydrofuran High-energy gamma rays used during radiation treatment of cancer produce low-energy electrons, which can cause single- and double-strand breaks in DNA. One goal of Arumainayagam's group's research at Wellesley is to further the understanding of radiation damage to DNA by studying the low-energy electron induced reactions of tetrahydrofuran, an analog for the sugar in the DNA backbone.

		Dora Carrico-Moniz, Chemistry Hepatitis C Virus NS3 Protease Domain:NS4A Peptide Complex (Lamarre, D. et al. 2003. An NS3 protease inhibitor with antiviral effects in humans infected with hepatitis C virus. Nature 426, 186-189.) The Carrico-Moniz lab is interested in the design and synthesis of small molecules of medicinal importance. Students in the Carrico-Moniz lab will be involved in research projects that are aimed towards the development of novel antitumor and antiviral agents.

		Don Elmore, Chemistry Personal website Antimicrobial peptide buforin II Snapshot of a molecular dynamics simulation of the antimicrobial peptide buforin II interacting with a lipid membrane. Students in the Elmore lab perform these simulations in conjunction with experimental labwork to probe the structure-function relationships of membrane proteins.

		Nolan Flynn , Chemistry Personal website N-Isopropylacrylamide When polymerized with a cross linking agent present, N-isopropylacrylamide forms a hydrogel, which shrinks and expels its contents when heated through the physiological temperature range. Students in the Flynn lab explore the temperature-dependent diffusion of macromolecules from N-isopropylacrylamide-based hydrogels.

		David Haines, Chemistry Personal website Exendin (Neidigh, J. W.; Fesinmeyer, R. M.; Prickett, K. S.; Andersen, N. H. 2001. Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle associated states. Biochemistry 40, 13188-13200.) NMR structure of exendin, a peptide found in gila monster venom that is a potential therapy for diabetes as it promotes a physiological response similar to that of GLP-1. Students in the Haines lab have synthesized several unnatural amino acids to study the function of these peptides.

		Gary Harris, Biological Sciences Personal website Phototropin1 (111 kDa) and phototropin2 (102 kDa) These plant blue light receptors are known to mediate a variety of physiological events, including stomatal opening, phototropism and chloroplast movement. The phototropins are membrane-associated proteins containing two LOV (light, oxygen, voltage) domains that bind flavin mononucleotide (FMN) chromophores and C-terminal serine/threonine kinase domains. Students in the Harris lab have attempted to identify proteins that physically interact with phototropin 1 using the techniques of co-immunoprecipitation and peptide mass fingerprinting.

		Jennifer Hood-DeGrenier Personal website FKBP12 and human TOR fragment bound to rapamycin (Choi, J., Chen, J., Schreiber, S.L., and Clardy, J. 1996. Structure of the FKBP12-Rapamycin Complex Interacting with the Binding Domain of Human FRAP. Science 273:239-242.) Rapamycin is a cell growth inhibitor that is used as an immunosuppressant and is being investigated as a cancer drug. It inhibits a central regulator of cell growth, the protein TOR, by forming a complex with TOR and another protein, FKBP12; this image depicts the structure of this complex, which was solved by X-ray crystallography. Research in the Hood-DeGrenier lab is investigating the basis of rapamycin hypersensitivity exhibited by a yeast cell cycle mutant.

		Nancy Kolodny, Chemistry Personal website A box of 216 water molecules The water molecule is ubiquitous in living systems and is the molecule whose protons most commonly are responsible for magnetic resonance (MR) images. Furthermore, water is the solvent for metabolites in organisms ranging from cyanobacteria to crayfish to mice. Students in the Kolodny lab have performed many MR imaging and spectroscopic studies on these living systems.

		Martina Koniger, Biological Sciences Personal website Arc6 (Stanislav Vitha, John E. Froehlich, Olga Koksharova, Kevin A. Pyke, Harrie van Erp, and Katherine W. Osteryoung. Plant Cell 15: 1918-1933.) A J-Domain protein related to the cyanobacterial cell division protein Ftn2 is crucial for proper chloroplast division. Students in the Königer lab have isolated and characterized a novel allele of arc6 which leads to the formation of 1-2 gigantic chloroplasts per mesophyll cell rather than the 70-120 small chloroplasts typically found in wildtype plants. The reduction in chloroplast number in this mutatant leads to a decreased ability to move chloroplasts in response to changes in blue light intensities.

		Julia Miwa, Chemistry Personal website GCN4 (O'Shea, E. K; Klemm, J. D.; Kim, P. S.; Alber, T. 1991. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254, 539-544.) NMR structure of the GCN4 leucine zipper, a DNA binding domain. Students in the Miwa lab have gained insight into the structure of proteins with unnatural amino acids by synthesizing and studying the molecular conformations of thioamide-containing analogs of GCN4.

		Kaye Peterman, Biological Sciences Personal website Sec14 (Sha, B.; Phillips, S. E.; Bankaitis, V.A.; Luo, M. 1998. Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol transfer protein. Nature 391, 506-510.) Crystal structure of Sec14, a yeast phosphatidylinositol transfer protein. Students in the Peterman lab have isolated and characterized a novel plant protein, Patellin1, which is closely related to Sec14 and appears to be important in plant cell division.

		Dennis Smith, Biological Sciences Personal website Epinephrine Epinephrine is secreted by the adrenal medulla and some nerves. It binds to adrenergic receptors and has a variety of actions, depending on the target organ. In the heart it speeds up the heart rate and the contractile force. Prolonged exposure triggers heart failure.

		Marc Tetel, Biological Sciences Personal website ER α bound to estradiol (Tanenbaum DM, Wang Y, Williams SP, Sigler PB. Proc Natl Acad Sci U S A. 1998, 11:5998-6003.) The Tetel lab studies how the ovarian steroid hormones, estradiol and progesterone, act in the brain to regulate gene expression and female reproductive behavior in rodents.

		Didem Vardar-Ulu, Chemistry Personal Website Negative Regultory Region of human Notch2 (Gordon WR, Vardar-Ulu D, Histen G, Sanchez-Irizarry C, Aster JC, Blacklow SC. Nat Struct Mol Biol. 2007 Apr;14(4):295-300) Before ligand-induced activation, Notch is maintained in a resting, metalloprotease-resistant conformation by a conserved Negative Regulatory Region that contains the activating cleavage site. Students in the Vardar-Ulu lab clone, express, and purify individual domains or domain combinations from this regulatory region and characterize them. They are also involved in designing small mutant proteins with enhanced functions.

		Andrew Webb, Biological Sciences Personal website Immunoglobulins Naturally occuring immunoglobulins have identical heavy chains and light chains giving rise to multiple binding sites with identical specificities for an antigen. For example the IgG molecule shown here has two identical heavy (blue) and two identical light (green) chains. Research in the Webb lab works with a monoclonal antibody that is designed to bind a marker on pancreatic cancer cells.

		Adele Wolfson, Chemistry Personal website Thimet oligopeptidase (Ray, K.; Hines, C. S.; Coll-Rodriguez, J.; Rodgers, D. W. 2004. Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization. J. Biol. Chem. 279, 20480-20489.) Crystal structure of thimet oligopeptidase (TOP), an enzyme involved in regulating neuropeptides. Students in the Wolfson group have characterized the structure-function relationships of TOP using kinetic studies, measures of protein stability, and site-directed mutagenesis.

The Biological Chemistry Advisory Committee currently is composed of Mary Allen, Director; Don Elmore, Jennifer Hood-DeGrenier, Kaye Peterman, Didem Vardar-Ulu, and Adele Wolfson.

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