2 New Faculty Members Join Biochemistry

Tijana Ivanovic and Maria-Eirini Pantelia have joined the Biochemistry department. Both of the new faculty members will begin at Brandeis in January 2016.

tijana_photoTijana Ivanovic, is currently a postdoc at Harvard Medical School.  Stephen C. Harrison is her advisor. She received her PhD in Virology from HMS and her BS in Microbiology and Molecular Genetics from UCLA.

Her research focuses on uncovering fundamental molecular mechanisms of virus translocation across biological membranes, in the distinct contexts of enveloped-virus membrane fusion and nonenveloped-virus membrane penetration.  She applies and develops advanced biophysical and biochemical approaches and combines them with those of virology, molecular biology and cell biology.

Dr. Ivanovic received a grant from the L’Oréal USA For Women in Science fellowship program in 2011.

pandeliaMaria-Eirini Pandelia‘s ‘scientific journey’ started from Greece, where she received her undergraduate degree in Physics from the University of Patras and master of sciences degree in applied Mathematics and Physics from the National Technical University of Athens. She carried out her graduate studies in Germany at the Max-Planck Institute (MPI) of Chemical Energy Conversion (formerly known as MPI for Bioinorganic Chemistry) and received her doctoral degree from the Technical University of Berlin. This was followed by 3 years as a postdoc at PennState University in the Bollinger/Krebs laboratory.

Her research lies in the interface of Chemistry, Biology and Physics with particular focus on the study of metalloenzymes. Her work encompasses the combination of spectroscopic and biophysical techniques together with structural biology and phylogenetics to address the modus operandi of metalloproteins and bioinorganic complexes. Her main expertise is in Mössbauer and EPR spectroscopies coupled to time-resolved kinetics (optical, FTIR) and redox potentiometry. She is interested in understanding how diverse enzymes carry out their bio-transformations and how reaction selectivity in homologous proteins is achieved.

Maria-Eirini’s work at Brandeis will be centered on delineating the mechanisms according to which metalloproteins involved in processes essential for life perform the activation of small (or larger) molecules, how the specific identity of the metals in the active sites allows their chemical diversion and selectivity and what the functional role of iron-sulfur clusters in proteins involved in DNA synthesis and repair is.






Phi Beta Kappa Elects 51 Division of Science Students

Phi_Beta_Kappa_KeyThe Brandeis chapter of Phi Beta Kappa recently elected 97 new members. Of the 97, at least 51 undergraduate students are majors in the Division of Science (Biochemistry, Biological Physics, Biology, Chemistry, Computer Science, Mathematics, Neuroscience, Physics and Psychology).

Congratulations to the following new Phi Beta Kappa members from the Division of Science:


Malia Barbra McAvoy
Yehonatan Otzar Meschede-Krasa
Juhee Park
Lior Rozhansky
Hanchen Zhao (double major with Chemistry)

Biological Physics

Abigail Rose Knecht


Ignatius Ang
Zachary Ian Fried
Jenna Leah Kahane
Ariel Jennifer Katz
Yang Li
Yixuan Liao
Alice Yuan Meng
Khang Vi Nguyen (double major with Chemistry)
Danielle Marie Quintin
Sarah Shin


Khang Vi Nguyen (double major with Biology)
Soobyung Park
Noam Isaac Saper
Hanchen Zhao (double major with Biochemistry)

Computer Science

Kenneth William Foner
Huy Quang Mai
Grady Berry Ward (double major in Mathematics)


Cameron Zhang Fen
Trevor Weiss Kafka
Linda Li
Huy Quang Mai
Stefan Stanojevic
Zhengyang Zhou
Daniel Jackson Kutner (double major in Physics)
Murielle Claire Tugendhaft
Grady Berry Ward (double major in Computer Science)


Jessica Allison Haley (double major with Psychology)
Kiera Gillian Sarill (double major with Psychology)



Wei Zhong Goh
Stefan Stanojevic
Daniel Jackson Kutner


Kyra Jordana Borenstein
Hannah Dvorah Caldwell
Nicole Danielle Cardona
Avi David Cohen
Annie Cui
Jason Michael Desimone
Emily Rose Friedman
Jonathan David Gilman
Clara Emily Gray
Cecilie Gromada
Sarah Jessica Hack-Chabot
Jessica Allison Haley (double major with Neuroscience)
Jessica Lynn Lieberman
Danielle Mizrachi
Emily April Mostow
Linda Sue Nakagawa
Talia Michelle Portal
Jenna Louise Rice
Kiera Gillian Sarill (double major with Neuroscience)
Aliza Naomi Shapiro

See full story on BrandeisNow.

Biochem BS/MS Application Deadline is May 1, 2015

Brandeis Juniors (class of 2016) in Biochemistry who are already working in a lab and are confident of a high GPA should take note of the Joint BS/MS Biochem  program at Brandeis. Application must be made to the graduate school by May 1 of your Junior year.  To apply, you will need approval of your lab PI and of the UAH (Dan Oprian).

Please be aware that this program requires a significant amount of effort, but may be to your benefit if you are already close to completing the requirements.

MRSEC Summer Undergraduate Research Fellowships (2015)

The Division of Science wishes to announce that, in 2015, we will offer  MRSEC Summer Undergraduate Research Fellowships for Brandeis students doing undergraduate research, sponsored by the Brandeis Materials Research Science and Engineering Center.The due date for applications  is February 24, 2015,  at 6:00 PM EST.MRSEC Summer Undergraduate Research Fellowships will provide $5000 in stipend support to allow students to do summer research in MRSEC labs (housing support is not included). Students who will be rising Brandeis sophomores, juniors, or seniors in Summer 2015 (classes of ’16, ’17, and ’18). No prior lab experience is required. A commitment from a Brandeis MRSEC member to serve as your mentor in Summer 2015 is required.The Division of Science Summer Program will run from May 26 – July 31, 2015. Recipients are expected to be available to do full time laboratory research during that period, and must commit to presenting a poster at the final poster session on July 30, 2015. Five positions are available.The application form is online (Brandeis login required). Questions that are not answered in the online FAQ may be addressed to Steven Karel <divsci at brandeis.edu>

Making a gold studded protein ring

PLEASE NOTE: the paper by Anthony et al. in Structure was subsequently retracted due to the discovery of research misconduct by its first author, see http://www.cell.com/structure/abstract/S0969-2126(14)00016-1.

In economically turbulent times gold is acquired and held onto as a stable, secure commodity – it’s the “gold standard”. Gold of course has been a source of wealth as a precious metal and source of beauty. Importantly, gold is an incredibly dense and malleable transition metal that maintains its beauty and strength over long time periods, existing as a stable pure solid. Gold has also been an important subject of study and use in life science applications as well as in the physical sciences and in the clinical realm – not only as a source for fillings or a bridge after the dentist deals with your teeth issues!

Kelsey Anthony, a doctoral student in the Brandeis Biochemistry program as well at the Quantitative Biology program, has been working with gold in the Pomeranz Krummel lab to study biopolymer structure. The properties of gold most important in these applications are that it is a pure and stable solid, forms monodisperse spheroidal aggregates, is electron dense, and has the property of anomalously scattering x-rays at specific wavelengths. All these properties combined make gold an optimal metal to be “visualized”. In her most recent application of gold, in press in the journal Structure, Kelsey collaborated with a group at the University of Osnabruek in Germany in the synthesis of a reagent conjugated with monodisperse gold clusters or nanoparticles (called AuNPtris-NTA, see figure) and employed this reagent to localize protein(s) of interest in large multi-protein assemblies.


The experiment most visually striking to demonstrate the utility of this new “gold reagent” involved attaching it to a protein that interacts with itself to form a ring shaped structure. When visualized using the electron microscope, the gold clusters or nanoparticles site-specifically attached to the protein appear as extremely dense black spots due to their significant scattering of electrons as a consequence of the gold’s electron dense structure.

In essence, Kelsey has created a stunning golden microscopic studded ring. Next up, employing this gold conjugated reagent in other new ways.

See: Anthony et al., High-Affinity Gold Nanoparticle Pin to Label and Localize Histidine-Tagged Protein in Macromolecular Assemblies, Structure (2014)

4th Annual Sprout Grants – Call for applications

Bring your research and entrepreneurial ambitions to life!

The Brandeis University Virtual Incubator invites member of the Brandeis Community (undergrads, grad students, postdoctoral fellows, faculty, staff) to submit an application for a “Sprout Grant”. These grants are intended to stimulate entrepreneurship on campus and help researchers launch their ideas and inventions from Brandeis to the marketplace.

This spring we will be awarding $50,000 to be shared amongst the most promising proposals.

Come get your questions about the Sprout grant answered at one of our upcoming information sessions.

Info sessions:

Tuesday      February 18th    1pm – 2pm

Tuesday      February 25th    10am – 11am

Thursday     February 27th    11am – noon

Tuesday      March 4th          11am – noon

All information sessions will be held in the Shapiro science center 1st floor library, room 1-03 (the glass walled room near the elevators).

Deadlines: Preliminary applications are due on Friday, March 7th

Benefits of participation:

  • Teams that are selected to submit full applications will be given assistance in further developing their ideas into an effective business pitch.
  • Sprout grant winners will be connected with an experienced mentor, and given further assistance in getting their ideas to market by the Office of Technology Licensing.
  • Previous winners have come from many departments: Neuroscience, Biology, Biochemistry, Physics and Computer Science. Some of the funded technologies have resulted in patent applications and are moving towards commercial development. Read more about previous winners from your department here: Sprout winners 2011, Sprout winners 2012, Sprout winners 2013.

For more information go to our website (http://www.brandeis.edu/otl/grants/index.html) or contact Melissa Blackman at melblack@brandeis.edu.

Tenure-track faculty position in Biochemistry

The Department of Biochemistry at Brandeis University invites applications for a tenure-track faculty position, to begin Fall 2014. We are searching for a creative scientist who will establish an independent research program and who in addition will maintain a strong interest in teaching Biochemistry at the undergraduate and graduate levels. The research program should address fundamental questions of biological, biochemical, or biophysical mechanism. Brandeis University offers the rare combination of a vigorous research institution in a liberal-arts college setting. The suburban campus is located 20 minutes from Boston and Cambridge and is part of the vibrant community of academic and biotechnology centers in the Boston area. The application should include a cover letter, curriculum vitae, statement of research accomplishments and future plans, copies of relevant publications, and three letters of reference. Applications will be accepted only through AcademicJobsOnline at https://academicjobsonline.org/ajo/jobs/3366. Additional inquiries may be directed to Dan Oprian, Professor of Biochemistry (oprian@brandeis.edu). First consideration will be given to applications received by December 1, 2013.

Brandeis University is an Equal Opportunity Employer, committed to building a culturally diverse intellectual community. We particularly welcome applications from women and minority candidates.

How bacteria resist fluoride

Fluoride anion is everywhere.  Released into water through the natural weathering of rocks, it’s present to the tune of 5 mM in toothpaste, 30 μM in Cape Cod bay, and 17 μM in Massell pond at Brandeis.

Fluoride levels in our environment (graph).001

Fluoride in the environment, measurements by Ashley Brammer (Miller lab)

Since F is ancient, ubiquitous and toxic to microbes, it’s not surprising that bacteria have evolved defenses to expel it from their cytoplasm.   In an article published in eLife on August 27, 2013, Randy Stockbridge, Janice Robertson, and Luci Partensky from Chris Miller’s lab describe one of these microbial defenses, a fluoride channel called Fluc.  The channel provides a pathway for F to exit the cell across the membrane at a rate of 107 ions per second, while rigorously excluding Cl in order to avoid catastrophic membrane depolarization. The world-record 10,000-fold selectivity isn’t the only remarkable aspect of Fluc, however. The Fluc channel is built on an antiparallel dimer scaffold, with one of the subunits facing the exterior of the cell, and the other facing the interior. Only one other modern-day membrane protein is known to dimerize like this, but the arrangement recalls the inverted structural repeats that are a common, important motif for membrane transporters. Inverted repeats are the product of an antiparallel dimer, like Fluc, that duplicated and fused eons ago.  The sequences drifted over time until the duplication was undetectable by sequence similarity, and the plethora of membrane transport proteins built on this plan was only discovered when the 3-D structures were solved. The Fluc family provides the opportunity to study microorganism resistance to an ancient xenobiotic, as well as membrane protein architecture from an evolutionary origin.

For more, you should read the paper:

Stockbridge RB, Robertson JL, Kolmakova-Partensky L, Miller C. A family of fluoride-specific ion channels with dual-topology architecture. eLife. 2013;2(0):e01084. PMCID: 3755343.

PS: If you’re wondering about the tea on the bar graph, tea plants accumulate F in their leaves.  Cheap teas, made from older tea leaves, actually carry a lot of F, and if you drink a couple quarts of lousy tea a day, you can give yourself skeletal fluorosis.

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