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Carrie Wilmot Laboratory [ Back ]

 
Contact Information:
 
Laboratory: 5-230 BSBE
Telephone: (612) 624-0141
 
Carrie Wilmot
wilmo004@umn.edu

Research Staff
 

 
Teresa De la Mora-Rey, PhD Postdoctoral Associate

I was born in Chihuahua, Mexico. I grew up in the border city of Cd. Juarez, Mexico. I graduated from the University of Texas at El Paso with a B.S. in Microbiology. After working for two years as a research assistant in the University of Texas at El Paso I decided to pursue a Ph.D. degree, which I recently completed (Jan 2008). I enjoy spending time with my husband, seeing different places -although I do not have enough time for traveling- dancing, and going to the movies. Besides working on my research, I have organized the weekly Structural Biology Journal Club, in which labs interested in structural biology get together to hear about each other’s research, and discuss the recent literature.
 
My Ph.D. research was focused on trapping the intermediates of the methylamine dehydrogenase reaction within crystals of the enzyme. Methylamine dehydrogenase catalyzes the conversion of methylamine to ammonia and formaldehyde. It is an 22 heterotetramer containing a novel cofactor, tryptophan tryptophylquinone (TTQ), derived from two modified tryptophan residues. I used X-ray crystallography to visualize the structural changes that occured during catalysis at the molecular level, and combined this with single crystal UV/visible spectroscopy to verify the identity of the intermediate. I am currently working on the structure of MauG, an unusual di-heme enzyme involved in the biosynthesis of the methylamine dehydrogenase TTQ cofactor.


 

Lyndal Hill, PhD Postdoctoral Associate

Lyndal, a native of Australia, will join the Wilmot lab mid-April 2008.

Brandon R. Goblirsch, B.S. Graduate Research Assistant

Brandon, a native of New Ulm, Minnesota, joined the Wilmot lab in Feb 2007.

His Ph.D. studies focus on chlorite dismutase, a novel heme enzyme that dismutes chlorite (a significant water pollutant) to chloride ions and molecular oxygen.


Valerie J. Klema , B.S. Graduate Research Assistant

Val who hails from Missouri, joined the Wilmot lab in Feb 2007.

Her Ph.D. studies focus on the molecular basis of 2,4,5-trihydroxyphenylalanine quinone biosynthesis in the enzyme copper amine oxidase.


Peder Cedervall, MS Junior Scientist

Peder, a native of Sweden, came to the Wilmot lab in Fall 2007 to carry out his Diploma research for his MS in Chemical Biology from Linkoping University, Sweden. He has subsequently remained in the Wilmot lab, and will join the PhD Program in Fall 2008.

His research focuses on solving the structures of methyl-coenzymeM reductase catalytic intermediates.


 

Joshua Goldford, Undergraduate Researcher

Josh, a Biochemistry Major at the U, joined the Wilmot lab in Jan 2008.

His research focuses on structural inhibition studies of copper amine oxidase and monoxygenases involved in siderophore synthesis in pathogenic bacteria.



 
Ed Hoeffner
Information Technology Professional / Manager
I ensure that the Kahlert Structural Biology Laboratory is running as smoothly and efficiently as possible. Keeping the X-ray generators and detectors running tops the list. After that come the computers owned by the crystallography faculty (around 20 Mac's and PC's altogether). Just about anything else that needs to get done tends to fall into my hands eventually. With the time that doesn't occupy, I have collected and processed X-ray data, and have recently begun to solve and refine protein structures. I've also done some software development attempting to determine protein electrostatic characteristics by evolving solutions to the equations involved.

Lab Members 2006
 






(left to right); Teresa De la Mora-Rey, Kelsey Newell, Nora Yucel, Carrie Wilmot, Bryan Johnson, Arwen Pearson, Ed Hoeffner



Past Research Staff


 
Arwen R. Pearson, PhD
Research Assistant Professor

 

Arwen has recently moved to the University of Leeds, UK, where she is an RCUK Academic Research Fellow in Protein Structure, Modelling and Design in the Institute for Molecular and Cellular Biology. Catch up with Arwen through her new website.

Before I came to Minnesota I was in grad school at The University of St Andrews in Scotland. I did my PhD studies under Prof. Garry Taylor on the human enzyme xanthine oxidoreductase. I arrived at Minnesota just after Carrie (May 2001) and was the only person in the lab for over a year. This meant I got to arrange everything in the lab so it made perfect sense to me. Now that we have graduate students, they keep moving things, so I guess my system wasn't as foolproof as I first thought!
 
Most of my time is spent working on methylamine dehydrogenase (MADH). I am trying to understand both the catalytic cycle of the enzyme (using single crystal microspectrophotometry) as well as the biogenesis of its protein derived cofactor, tryptophan tryptophylquinone (TTQ). In addition to MADH I am also involved in structural studies of tRNA synthetase and xanthine oxidoreductase.
 
Over the last few years I have become involved in the American Crystallographic Association Young Scientist Special Interest Group (YSSIG). We organize both sessions and socials at the ACA national meetings and so far it has been a lot of fun.
 
After over 3 years here I have finally come to terms with the cold winters by learning to snowboard. I'm still not very good but I have a great time.



 
Bryan J. Johnson, B.A.
Graduate Research Assistant

Bryan now works at R&D Systems in the Twin Cities, MN.

I was born in Grand Rapids, MN. I received my Bachelor's degree in Chemistry from St. John's University and am currently working toward my Ph.D in structural biology at the University of Minnesota. Previous research experience included synthesis of organic model complexes with copper. My hobbies include music, mountain biking, snowboarding, and electronics.
 
Copper-containing amine oxidases are quinoenzymes that catalyze the oxidation of primary amines to aldehydes through the activation of molecular oxygen. The physiological role of amine oxidases in higher organisms is not well known, but its activity in humans is linked congestive heart disease, diabetes and the inflammatory response. While the reductive half-reaction of amine oxidase has been well characterized the oxidative half has not. My research includes trapping intermediates of the oxidative-half reaction in crystals to probe gas (oxygen) binding. I use a combination of X-ray crystallography and single crystal microspectrophotometry to study this. Our hypothesis is that molecular oxygen binds off of the active site copper and is initially reduced directly by the amine reduced topaquinone protein derived cofactor



 
Nora Yucel
High School Senior
 

Nora is now a sophmore at the University of Chicago, where she hopes to major in Biochemistry. She is continuing her research using crystallography to study the light, oxygen or voltage (LOV) photoreceptor domain in the laboratory of Keith Moffat.

I am a soon to graduate senior at Edina High School in Edina. I became connected to Dr. Wilmot through a school program called Mentor Connection, which I have been taking part in in lieu of going to the last part of my school day. Working in the Wilmot Lab since October 2005, I have enjoyed my fair share of utter confusion mixed with occasional showers of understanding, the latter making the former all worth it.
 
Everything started one 9-month span in 11th grade when I realized I actually liked my AP Biology class and couldn't for the life of me understand why on earth the subject would ever elicit groans from 17-year olds. This same sentiment lead me to take a cell-biology class at Harvard Summer School (along with creative writing) where I learned that I was barely skimming the surface of the word "biology" but still wanted to dive in. Thus I began my highly scientific investigation of U of M faculty lists, bravely emailing those whom I had never emailed before and interviewing anyone who replied in kind.
 
So it went. Through happenstance and a few well-placed, sunlit lab tours I arrived at my current destination. I have since learned the joys of watching (or waiting for) tiny crystals to grow and uncovering more information about X-ray crystallography, methylamine dehydrogenase and amicyanin than I could have ever thought possible a year ago. I am currently working with Teresa De la Mora-Rey to isolate a methylamine dehydrogenase mutant, and catch the reaction intermediates of the copper active site of amicyanin. When I'm not doing this I enjoy writing, playing violin, having fun in a safe environment and eagerly anticipating my first semester as a University of Chicago freshman.



 
Kelsey Newall B.S.
Graduate volunteer

Kelsey now works at R&D Systems in the Twin Cities, MN.

I was born here in Minneapolis , MN and have recently graduated from the University of Minnesota with a B.S. in Biology. I began working in the Wilmot lab under the instruction of Arwen Pearson as an undergraduate directed research project. I have since finished the project and continue to spend two days a week exploring the field of structure biology. I arrived in the lab with no previous lab experience and have learned more in the past six months than could have ever been imagined. I am planning on spending the next year relaxing and researching during a year off, after which I will hopefully be attending medical school.

I began my time in the lab working under Arwen Pearson on Human Xanthine Oxidoreductase, however will be continuing my studies under Bryan Johnson looking at cofactor biosynthesis in Hansenula polymorpha (HPAO).


 

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