Coon Lab People

Name Room Phone Position Email
s
 Joshua J Coon 3309 3-1718 Professor jcoon@chem.wisc.edu
s
 David Good 3223 890-0763 NIH Predoctoral
Fellow 		dgood@wisc.edu
april
 April Jue 3223 890-0763 Graduate Student ajue@wisc.edu
jason
 Jason Russell 3223 890-0763 Graduate Student jrussell@chem.wisc.edu
s
 Graeme McAllister 3223 890-0763 NIH Predoctoral
Fellow 		graeme.mca@gmail.com
s
 Doug Phanstiel 3223 890-0763 Graduate Student doug.phanstiel@gmail.com
s
 Danielle Swaney 3223 890-0763 NIH Predoctoral
Fellow 		swaney@wisc.edu
aarron
 Aaron Ledvina 3223 890-0763 Graduate Student arledvina@gmail.com
s Justin Brumbaugh 3223 890-0763 NSF and NIH Predoctoral Fellow brumbaugh@wisc.edu
s Michael Williams   890-0763 Undergraduate
Graphic Design &
Illustration

mpwilliams@wisc.edu
           


Joshua Coon
Assistant Professor of Chemistry
Central Michigan University (B.S.)
University of Florida (Ph.D.)
University of Virginia (Postdoctoral Fellow)
Room: 3309
Telephone: (608) 263-1718

Awards:
Beckman Young Investigator Award (2007)
Eli Lilly and Company Young Investigator
American Society of Mass Spectrometry Research Award (2007)
Named one of tomorrow's PI's by Genome Technology (2006)
NIH – National Research Service Award Postdoctoral Fellow (2003 – 2005)

David Good
I graduated with a B.S. in Chemistry from Hampden-Sydney College in Virginia in 2005. I am currently a second year Analytical Chemistry student in the Coon lab.

My research focus is on using biological mass spectrometry for protein analysis. More specifically, my projects involve using separations technology coupled with tandem mass spectrometry [employing ion-ion chemistry; e.g. Electron Transfer Dissociation (ETD)] for disease biomarker identification and characterization.

April Jue
April Jue is a first year graduate student in the lab. She graduated in 2004 from the University of North Carolina at Chapel Hill with a B.S. in biochemistry. Her undergraduate research was conducted in Dr. Gary Glish’s lab where she utilized mass spectrometry to investigate peptide dissociation pathways. Before beginning graduate school, she spent six months at the Federal Bureau of Investigation as a visiting scientist with the Counterterrorism and Forensic Science Research Unit. April is using ETD to analyze fixed-charges on peptides and proteins.

Jason Russell
I am a 1st-year Analytical Chemistry graduate student originally from Eastern Iowa.  I received a bachelor's degree in Biology from the University of Northern Iowa in 2002.  I spent the next four years working in industry as a chemist for GELITA USA, a gelatin manufacturer located in Sioux City, IA.  While working at GELITA, I began work on a Master's degree in Chemistry at the University of South Dakota.  I received a Master's degree in 2007 while working in the lab of Dr. Miles Koppang. Our research focused on electrochemical detection of amino acids and the study of gas-phase rearrangements of ionic liquids using electrospray ionization mass spectrometry.  My current research focuses on developing liquid chromatographic and mass spectrometric methodology to allow precise quantitation of protein and peptide expression levels during human embryonic stem cell differentiation.

Graeme McAllister


My primary goal is advancing electron transfer dissociation (ETD) equipped mass spectrometer instrumentation. There are two sub-categories to this goal: (1) upgrading and optimizing mass spectrometer equipment which is already capable of performing ETD, and (2) adapting additional mass spectrometer equipment to be compatible with ETD. There have already been two significant successes - one for each sub-category.

During the late spring of 2006, I collaborated with another member of my lab group (Danielle Swaney) on a project that had the goal of converting non-dissociated electron transfer (ET) products into c and z-type product ions (i.e. the typical ETD product ions). I adapted the instrument (an LTQ equipped with a prototype Thermo Electron ETD package) to do gentle CAD of the electron transfer product. At low activation energy, we found that the ET product ions could be converted in c and z-type ions without generating typical CAD ions, which would have cluttered our spectra. By adding in this additional activation step, we were able to generate additional fragment ions and produce spectra that were far informative.

In the fall of 2006, I adapted an LTQ-Orbitrap hybrid mass spectrometer to allow for ETD. Mass analysis with an Orbitrap produces spectra that are significantly more resolved and with better mass accuracy. Do to spacial complications, I wasn't able to mount a CI source on the rear of the instrument (i.e. how the current LTQ's have been adapted to allow for ETD). Instead I used the same atmospheric pressure inlet, on the front of the instrument, to inject both the cations and the reagent anions. To utilize the same inlet for both ions, I had to pulse the sources. This work drew heavily from previous research done by the McLuckey group at Purdue. The resulting spectra, which were significantly more resolved and had much better mass accuracy, allowed for better fragment identification. In particular highly charged fragment ions could now be identified which would have been impossible with QLT mass analysis.

On a personal note, I was able to spend the summer of 2006 as an intern for Thermo Electron. I worked closely with Jae Schwartz and John Syka developing software for the Thermo commercial LTQ-ETD package. I'm extremely grateful for this opportunity, which was made possible through the generosity of Thermo Electron and the Biotechnology Training Program at the University of Wisconsin-Madison. Thanks to my time spent at the company - I am far more adept at executing these instrumentation projects in a timely and effective manner.

Doug Phanstiel
I received a B.S. in biochemistry and cell biology from the University of California, San Diego. I am a first year graduate student in analytical chemistry. My research focuses on using mass spectrometry to identify post-translational modifications of proteins isolated from human embryonic stem cells. In addition to identification we are interested in quantitatively describing changes in expression and modification of these proteins in response to different cell growth conditions.

I am also involved in other projects implementing physical and/or software modifications to our LTQ mass spectrometer in order to enhance its protein characterization capabilities. Consecutive gas phase reactions have the ability to improve fragmentation as well as provide novel information about the peptides or proteins of interest. I am working on methods incorporating a number of different reactions in an intelligent and data dependent manner in an effort to increase efficiency of fragmentation.

Danielle Swaney
I am a second year graduate student in the chemistry department and am developing methods for identification and quantitation of protein phosphorylation.  I am from the pig and corn capital of the world Iowa).

Aaron Ledvina

I recieved a B.S. in chemistry and physics from Carthage College in May of 2006.  I am currently a first-year graduate student inAnalytical Chemistry in the Coon group at UW-Madison. My research interests include implementation of new concepts on andadvancement of the various instruments found in the Coon Lab.  My prior work/internship experiences include time with S C Johnson, Modine, and Henkel surface technologies.  When not in lab, I enjoy fishing, hunting, kayaking, and ultimate frisbee.  I am origionally from New Berlin, WI.

Justin Brumbaugh
Human embryonic stems (ES) cells are unique in that they have the capacity to differentiate into any specialized cell lineage, a characteristic termed pluripotency.  For this reason, human ES cells hold enormous potential, both for fundamental science and for therapeutic purposes.  Understanding how stem cells maintain the pluripotent state and are driven to differentiate into different cell types is key for future research and medical applications.  To this end, my work brings together developmental biology and mass spectrometry to study pertinent factors in human ES cells. 
Coupling high mass accuracy analyzers to emerging fragmentation techniques, namely, Electron Transfer Dissociation (ETD), enables us to determine not only amino acid sequence, but also post-translational modifications (PTMs) for a given peptide.  Thus far, we’ve focused mainly on epigenetic changes that occur during differentiation by tracking PTMs on histone H4.  Unique to our approach is the ability to identify combinatorial patterns (i.e. we detect distinct arrangements of modifications on the histone tail such that we can study each modification in the context of those around it).  A further goal is to track both post translational modification and binding partners for transcription factors important to pluripotency. 
My background is largely based in biochemistry.  I graduated from Penn State University with a B.S. in biochemistry and molecular biology (chemistry minor).  My undergraduate thesis work focused on cell wall structure in E. coli.  Afterwards, I traveled to Germany on a Fulbright Scholarship, where I spent two years at the European Molecular Biology Institute (EMBL) developing FRET based probes for kinase signaling. 

Katie Zastrow
 Katie is a second semester junior undergraduate at the University of Wisconsin- Madison.  She is majoring in Biochemistry and is planning to graduate in the spring of 2008.  Currently, she is assisting Danielle Swaney in the lab.


Michael Williams
 Michael is an undergraduate majoring in art and graphic design. At the Coon Group, he is performing web, graphic design, and illustration duties.