Jozafina Milicaj Receives PhD

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Dr. Jozafina Milicaj 

Dr. Jozafina Milicaj recently defended her Ph.D. and presented her work entitled, “Biophysical Exploration of Heptosyltransferase I for Potent Inhibitor Discovery.” Jozie started at Wesleyan University in 2015 after completing her BA in Chemistry at Manhattanville College where she was heavily involved with the American Chemical Society chapter and even holding the position as president for her senior year.  Jozie’s undergraduate research project was focused on analytical chemistry and the quantification of antioxidants from açaí berry sources through various extraction methods and UV-Vis radical capture assays. Upon starting at Wesleyan University, Jozie joined the research lab of Dr. Erika Taylor and began working on projects pertaining to Heptosyltransferase I substrate biosynthesis and optimization. Her projects then shifted to understanding and biophysically characterizing HepI and other glycosyltransferases like MshA for the purposes of inhibition of HepI. Having completed her degree at Wesleyan, Jozie will soon be starting her career in industry at Ginkgo Bioworks, a biotech company in Cambridge that professes in novel protein engineering where she will be characterizing and kinetically examining new proteins of interest.

Dr. Colin Smith Receives CAREER Grant from National Science Foundation (NSF)

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Colin Smith, Professor of Chemistry

“Dynamics of Computationally Designed Fluorescent Proteins”

The goal of the research is to study and optimize the movement of microscopic, computationally designed proteins that use light to track the locations of biological molecules and reveal how living organisms work. While the structure of a protein is almost always necessary for function, it is often not sufficient. This project focuses on the critical but often neglected role of protein motion in enabling absorbance and reemission of light, a process known as fluorescence. We will first determine which protein shapes either enhance or inhibit fluorescence through detailed analysis of computer simulations and extensive experimental structural characterization. Second, we will test our models through redesign and experimental examination of brighter fluorescent protein variants. As part of these efforts, we will develop a general-purpose computer algorithm that enables rapid evaluation of how thousands of potential mutations affect the shape of the protein. Third, we will investigate the structural determinants of other important properties like the ability of the protein to prevent or facilitate switching fluorescence on and off. The ultimate aim of this project is to develop a detailed understanding of how these fluorescent proteins can be redesigned to make them truly useful tools for biological research. This will enable the creation of even more advanced versions of these and other protein machines (like enzymes) that can also help in the manufacture and recycling of materials at the chemical level.

 

 

Chemistry Major Elected to Phi Beta Kappa

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Fall 2021 elections to Wesleyan’s Gamma Chapter of Phi Beta Kappa have been announced, and it is with great pleasure that we recognize Julia Lynne Lanfear.

To be elected, a student must first have been nominated by the department of his or her major. The student also must have demonstrated curricular breadth by having met the General

Education Expectations and must have achieved a GPA of 93 or above.

The emblem contains the three Greek letters “Phi,” “Beta,” and “Kappa,” which are the initials of the Greek motto, Philosophia Biou Kybernetes, or “the love of wisdom is the guide of life.”

 

Julia Lynne Lanfear, 2022
Biology, Chemistry 

Elected students will be honored at an induction ceremony on Wednesday, December 8, 2021 at 4:30p.m. in Allbritton 311.

Chemistry Alumnus Jessica Garcia Awarded Eastman Chemical Company Fellowship

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Jessica Garcia, a 2021 graduate of the BA/MA program in Chemistry, was recently awarded a fellowship through the University of North Carolina. The Eastman Chemical Company Fellowship program is a newly established award bestowed to first year graduate students at UNC for their committed effort to enhance the departmental mission to create a diverse and inclusive community. Sponsored by the Eastman Chemical Company, Eastman Fellows receive a stipend that supports the continuation of their contributions to the Carolina Chemistry community.  Jessica is among six students who were awarded this prestigious fellowship. Join us in congratulating her on this momentous achievement!

Personick Wins Silver (and more) at USRowing Masters National Championships

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Dr. Personick & teammates

From August 12-15th, Prof. Personick competed at the USRowing Masters National Championships on Melton Lake in Oak Ridge, Tennessee. The weather was hot, but the water was flat and cold—perfect for racing and keeping cool. Her team, Riverfront Recapture, won medals in 46 events – 24 gold, 11 silver and 11 bronze – a team record. After a fog delay each morning, Prof. Personick raced to win one silver medal (women’s open B four with coxswain*) and three bronze medals (women’s club A four with coxswain, mixed AA four with coxswain, and mixed B eight). She also finished fourth in the women’s open A four with coxswain and fifth in the women’s open A single sculls.

All of these finishes contributed points to Riverfront’s success in the team points competitions. The team won the men’s points trophy and finished second for club points, third for overall points (out of 112 teams), and second for the efficiency competition (points per athlete). Overall, it was a great success, and the team is now looking forward to the fall racing season!


Dr. Personick & teammates


Dr. Personick 


Medals & Hat


Dr. Personick’s team 


Melton Lake in Oak Ridge, Tennessee


Melton Lake in Oak Ridge, Tennessee

Results: https://herenow.com/results/#/races

Pictures: https://www.row2k.com/gallery/index.cfm?year=2021&category=Masters%20Nationals

* Letters indicate the average age of the crew: AA = 21-26, A = 27-35, B = 36-42

Dr. Benjamin Elling Joins the Chemistry Department

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The Chemistry Department is delighted to welcome Dr. Benjamin Elling as an Assistant Professor of Chemistry. His recently renovated lab, in the space formerly occupied by Albert J. Fry, will investigate new methods to synthesize and reprocess polymers. This semester he will be teaching CHEM 373, an upper-level course on polymer chemistry.

Professor Elling received his BA in chemistry from Cornell University, where he synthesized polymers for anion exchange membranes in the lab of Geoff Coates. He then attended Stanford University, where he became the first PhD student of Yan Xia and developed methods for sequence-specific polymerization via the ring-opening metathesis of substituted cyclopropenes. Prior to his appointment at Wesleyan, Professor Elling was a postdoctoral scholar in the lab of Professor Will Dichtel, where he designed new covalent adaptable networks and investigated strategies for mixed plastic compatibilization.

Here at Wesleyan, Professor Elling will combine his interests in synthetic methods development and sustainability. His lab will focus on leveraging strain energy to create polymers capable of controlled degradation, reprocessing thermosets through novel exchange chemistries, and incorporating renewable building blocks such as carbon dioxide into materials. The Chemistry Department is very pleased to have him join us.

Andrea Lee Receives PhD

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Dr. Andrea Lee

Dr. Andrea recently defended her Ph.D. dissertation entitled “Examining Chromium(III)-based Contrast Agents for Use as a Model for Understanding Prototropic Exchange in ParaCEST MRI Contrast Agents.” Andrea started at Wesleyan University in 2014 after graduating with honors from the University of New Haven where she received a B.S. in Forensic Science and a B.S. in Chemistry. Her undergraduate thesis work focused on analyzing the triglycerides in biofuel made from acorns using HPLC with detection by FT-IR and UV-Vis. Upon starting at Wesleyan University, Andrea joined the research lab of Professor Westmoreland and worked on many research projects exploring various transition metal-based MRI contrast agents and their properties in aqueous solutions. She also received many opportunities as a teaching assistant which included taking on many responsibilities in the Introductory Chemistry Laboratory. She was also awarded the Tishler Teaching Award in 2018. This fall, Andrea will be starting as an Assistant Teaching Professor at Drew University where she will be teaching Analytical Chemistry.

Dr. Andrea Lee


Tom Lee


Dr. David Westmoreland


From left to right: Kimberly Lee, Terrie Tin, and Samantha Lee


Dr. Andrea Lee and Dr. David Westmoreland


A captive audience


From top to bottom, left to right: Eric Zanderigo, Kaylah Medvec, Annika Velez, Dr. David Westmoreland,
Dr. Andrea Lee, Jozafina Milicaj, Angelika Rafalowski, Dr. Alison O’Neil, Dr. Colin Smith
Sean McDarby, Mohammed Ullah, Oliver Cho, Kat Blejec


Celebratory cake

From left to right: Tom Lee, Kimberly Lee, Dr. Andrea Lee, Terrie Tin, and Samantha Lee

 

Chemistry Major Demonstrates Flimsiness of Amherst Construction

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In a baseball game late in the spring semester, senior Chemistry major Dylan Judd shows that the Amherst fence is no match.  Dylan emerged unscathed and is now the only Wesleyan chemist we know who has gone viral (over 101,000 views and counting).  When he isn’t dispatching physical barriers, he works with Prof. Personick using nanoparticles to catalyze organic reactions.

 

Dr. Suara Adediran Publishes Paper in Biochimica et Biophysica Acta (BBA) – Proteins and Proteomics

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Dr. Adediran and co-authors Michael J. Morrison and R.F. Pratt have published a paper in Biochimica et Biophysica Acta (BBA) – Proteins and Proteomics. The title is “Detection of an Enzyme Isomechamism by Means of the Kinetics of Covalent Inhibition.”

Unlabelled Image

Abstract

Turnover of substrates by many enzymes involves free enzyme forms that differ from the stable form of the enzyme in the absence of substrate. These enzyme species, known as isoforms, have, in general, different physical and chemical properties than the native enzymes. They usually occur only in small concentrations under steady state turnover conditions and thus are difficult to detect. We show in this paper that in one particular case of an enzyme (a class C β-lactamase) with specific substrates (cephalosporins) the presence of an enzyme isoform (E′) can be detected by means of its different reactivity than the native enzyme (E) with a class of covalent inhibitors (phosphonate monoesters). Generation of E′ from E arises either directly from substrate turnover or by way of a branched path from an acyl-enzyme intermediate. The relatively slow spontaneous restoration of E from E′ is accelerated by certain small molecules in solution, for example cyclic amines such as imidazole and salts such as sodium chloride. Solvent deuterium kinetic isotope effects and the effect of methanol on cephalosporin turnover showed that for both E and E′, kcat is limited by deacylation of an acyl-enzyme intermediate rather than by enzyme isomerization.

The full text of the paper can be found at: https://www.sciencedirect.com/science/article/abs/pii/S157096392100087X

 

 

Dr. Colin Smith Receives NIH Grant

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Colin Smith, Professor of Chemistry

The Smith Lab studies protein structure and dynamics using a combination of computer simulation and nuclear magnetic resonance (NMR) spectroscopy. They are particularly interested in optimizing the dynamics of computationally designed proteins and understanding how mutations allosterically affect the functions of natural proteins.

To advance the understanding of atomic-level mechanisms behind critical protein functions like enzyme catalysis and allosteric regulation, it is important to first elucidate a true representation of the protein in solution. In an effort to achieve this long term goal, Dr. Smith will use the recently developed Kinetic Ensemble approach to transform the way in which nuclear magnetic resonance (NMR) data is computationally modeled to solve protein structures and measure protein motions. NMR is one of the most powerful techniques for elucidating the structure and dynamics of proteins. It enables their study in solution (unlike X-ray crystallography) and can capture critical structural rearrangements as they happen at room temperature (unlike cryo-electron microscopy). However, despite these advantages, there have been relatively few practical improvements to one of the foundational aspects behind the way protein structures are solved, namely the calculation of interatomic distances from nuclear Overhauser effect (NOE) experiments. Such methods have remained largely qualitative, resulting in large uncertainties in the atomic positions for most NMR structures. Also, the field has almost completely ignored how angular motion and kinetics affect the NOE, resulting in atoms appearing much further away from one another than they actually are. To overcome these significant deficiencies, Dr. Smith and his team will implement and test new Kinetic Ensemble-based refinement algorithms that are considerably more accurate and physically realistic than previous approaches, accounting for both angular motion and kinetics. To eliminate a significant fraction of the systematic and random structural errors resulting from poorly quantified NMR spectra, they will also integrate advances made by the FitNMR peak quantification software recently developed by their lab. These methods will be used to create better experimental NMR structures, more exhaustive models of side chain dynamics, and determine differences between solution and crystal states with unprecedented detail. This work will allow much more accurate determination of the structural dynamics in parts of the protein exhibiting significant fluctuations, including protein active sites, regulatory regions, and hidden binding sites. Such knowledge will advance our fundamental understanding of protein biophysics and facilitate rational design of new therapeutics.

Funding for this R15 Grant is provided by National Institute of General Medical Sciences (NIGMS).