Faculty Research Projects

Biological Chemistry students are involved in active research collaborations with chemistry and biology faculty members.

Listed below are faculty who are involved in biological chemistry research at Wellesley along with the picture of a molecule related to their work.  Follow the link for each faculty member to learn more about the work in their research lab.

You can also read about faculty research interests in this booklet.

Mary Allen, Biological Sciences
Image of early biofilm formation by motile unicellular cyanobacteria

The Allen lab is currently studying biofilm formation in cyanobacteria.  We are observing biofilms growing in flow chambers using confocal microscopy and assaying for quorum sensing molecules.  Differences in motile and non-motile strains and phototaxis abilities are being analyzed.

 

Chris Arumainayagam, Chemistry
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.

Barbara Beltz, Neuroscience
The neurogenic niche

The Beltz lab is interested in the production of new neurons in the adult brain, and particularly in the neuronal stem cells that initate the process.  We have found that these stem cells are not self-renewing, and our data strongly suggest that the hematopoietic (blood forming) system replenishes the stem cell pool.  Our current work is therefore focused on defining the molecular and cellular relationships between teh hematopoietic system and the lineage of cells that produces the adult-born neurons.
 

Dora Carrico-Moniz, Chemistry
Hepatitis C Virus NS3 Protease Domain:NS4A Peptide Complex

(Structure from:  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.
 

Louise Darling, Biological Sciences
Green fluorescent protein
(Structure from:  Ormo, M. et al.  1996.  Crystal structure of the Aequorea Victoria green fluorescent protein.  Science.  273, 1392.)
The discovery, characterization and engineering of GFP have revolutionized the way we view (literally) proteins in living cells.  The Darling lab uses GFP and other fluorophores to label and monitor the movement, mobility and interactions of proteins in cells.  We are currently investigating protein-protein interactions between cardiac ion channels and their contribution to maligant arrhythmias and sudden cardiac death.

Donald Elmore, Chemistry
Molecular dynamics simulation of four buforin II peptides

(Structure from:  Elmore. 2012. Insights into buforin II membrane translocation from molecular dynamics simulations. Peptides. 38:357.)
As microbial resistance to antibiotics increases, antimicrobial peptides provide a promising alternative to conventional therapeutics.  Students in the Elmore lab use a variety of experimental techniques and computational methods to improve our understanding of how these peptides work on the molecular level.  


Nolan Flynn , Chemistry
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
Exendin

(Structure from:  Neidigh, J. W. et al. 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
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.

Michael Hearn, Chemistry
Antitubercular drug candidate

With one third of the world’s population infected, tuberculosis represents a global public healthcrisis. Researchers in the Hearn laboratory are investigating new approaches to antitubercular drug design and discovery using the methods of synthetic organic chemistry.

Vanja Klepac-Ceraj, Biological Sciences
Research in the Klepac-Ceraj lab focuses on the succession, stability and resilience of microbial communitites as well as microbe-microbe interactions.
 

Nancy Kolodny, Chemistry
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
Arc6

(Structure from:  Vitha, S. et al. 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
GCN4

(Structure from:  O'Shea, E. K. et al. 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.

Megan Nuñez, Chemistry (Starting at Wellesley Fall 2013)
Artistic rendering of DNA

Students in the Nuñez lab use a variety of chemical, physical and biochemical tools to answer biological questions.  Some projects investigate DNA damage, particular the dynamics and thermodynamics of DNA with small base lesions, while others use atomic force microscopy and other techniques to examine bacterial predation in biofilms.

 

Kaye Peterman, Biological Sciences
Sec14

(Structure from:  Sha, B. et al. 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.

 

 

 

Joanne Pratt, Olin College of Engineering
RASSF1A

(Structure from:  Foley et al.  Dynamics of RASSF1A/MOAP-1 association with death receptors.  Mol Cell Biol.  2008, 14:4520-35.)
Computer model of amino acids 15-102 of RASSF1A, a tumor suppressor protein that is silenced by promoted methylation in many types of cancer cells.  Students in the Pratt lab study the role that RASSF1A plays in promoting apoptosis (cell death).  
 


Marc Tetel, Neuroscience
ER α bound to estradiol

(Structure from:  Tanenbaum D. M. et al. 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
Negative Regultory Region of human Notch2
(Structure from:  Gordon W. R. et al. 2007.  Nat Struct Mol Biol. 14:295-300)
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
Immunoglobulins

Naturally occurring 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
Thimet oligopeptidase

(Structure from:  Ray, K. et al.  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, and how the enzyme is regulated in brain.
Current projects involve regulation of this and other neuropeptidases in prostate cancer cells.

Contact Us

Contact Us

Director:
Don Elmore (Chemistry)
(781) 283-3171
delmore@wellesley.edu

 

Biological Chemistry Advisory Committee:
Melissa Beers (Biological Sciences)

 

Louise Darling (Biological Sciences)

 

John Goss (Biological Sciences)

 

Don Elmore (Chemistry)

 

Vanja Klepac-Ceraj (Biological Sciences)

 

Megan Núñez (Chemistry)

 

Elizabeth Oakes (Chemistry)

 

Kaye Peterman (Biological Sciences)

 

Mala Radhakrishnan (Chemistry)

 

Marc Tetel (Neuroscience)

 

Didem Vardar-Ulu (Chemistry)

 

Adele Wolfson (Chemistry)