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Chemistry

James Lipchock

Assistant Professor of Chemistry
Education
  • Bachelor of Arts, ACS-Certified Chemistry and Physics, 2004
  • McDaniel College, Westminster, MD
  • Master of Science, Biophysical Chemistry, 2006 
  • Yale University, New Haven, CT
  • Doctor of Philosophy, Biophysical Chemistry, 2010
  • Yale University, New Haven, CT
Teaching

For as long as I can remember I have had a passion for teaching. My experiences as an undergraduate at a small liberal arts college made me eager to return to this environment as a professor. My love for chemistry began in my sophomore year of high school and slowly evolved into my interdisciplinary interests as a biophysical chemist. While my teaching and research centers around biological molecules and incorporates spin physics and high level mathematics, I view all that I do from the lens of a chemist and believe the quantitative and critical thinking skills developed as a chemistry major prepare a student for a wide range of careers, both inside and out of science. 

While every field requires some memorization, what has drawn me to chemistry from the beginning is the ability to apply basic principles to answer new questions. My interest in biology began when I realized I could apply these same chemical principles to understand and predict the behavior of large biomolecules. My goal as a teacher is to help students fully understand important chemical principles and to learn to apply them to novel questions in any field that excites their passions.

I routinely teach General Chemistry I and II lecture and laboratory (CHE 111 and CHE 112). Every spring I also offer Chemistry of Biological Compounds (CHE 303). In the fall I alternate between a special topics course in biophysical methods and a GRW course entitled “Ethics and Profit in Globalized Medicine”. Please refer to the course catalog for additional information about these courses or stop by my office to chat.

Professional Experience
  • Assistant Professor of Chemistry, 2012-Current
  • Washington College, Chestertown, MD
  • Adjunct Professor of Chemistry, 2011-2012
  • Philadelphia University, Philadelphia, PA
  • Adjunct Professor of Chemistry, 2012
  • Delaware County Community College, Media, PA
  • Lecturer in Chemistry, 2011
  • Ursinus College, Collegeville, PA
  • Postdoctoral Researcher, 2010-2011
  • University of Pennsylvania, Philadelphia, PA

Research

The research in my lab is geared at understanding the function of biomolecules through enzymology and determination of their structure and dynamics. Given the interdisciplinary nature of my research, students working in my lab learn a wide range of techniques, from DNA cloning and mutagenesis to protein expression and purification, kinetics, multidimensional protein NMR spectroscopy and much more. If these techniques sound interesting to you, please read more about the projects below that are currently being explored in my laboratory.

Mechanistic Studies of Phosphohistidine Phosphatase 1

Phosphohistidine phosphatase 1 (PHPT1) is a human enzyme responsible for removing a phosphate group from phosphohistidine residues present on proteins. Unlike most known phosphatases, the phosphohistidine linkage results from a N–P bond, rather than an O–P bond. Given this chemical difference, the mechanism of phosphohistidine phosphatases is believed to be distinct from other known phosphatases. We are interested in better understanding the reaction mechanism of this novel class of enzymes and characterizing the structure of the enzyme-substrate complex.

Structure and Dynamics of the Vaccinia H1-Related Phosphatase

Vaccinia H1-related phosphatase (VHR) is a human dual specificity phosphatase capable of dephosphorylating phosphotyrosine, phosphoserine and phosphothreonine residues in proteins. It is known to play important roles in immune response, mitosis and much more. We are interested in better understanding the impact of phosphorylation at tyrosine 138 on the activity and substrate recognition of VHR, as well as characterizing the motion of active site loops.

Bringing NMR Dynamics to the Undergraduate Curriculum

Many undergraduate students are aware of the power of NMR spectroscopy for characterizing organic molecules and even structure determination of proteins and nucleic acids, but the use of NMR spectroscopy to investigate biomolecular motions is often overlooked in the undergraduate curriculum. This is unfortunate because this is arguably the most powerful application of NMR spectroscopy, unmatched by any other technique. I am interested in developing laboratory experiments appropriate for the undergraduate level that would introduce students to this important and active area of research.

Research Opportunities for Students

I am always eager to have hardworking, enthusiastic students join my lab for summer research fellowships, Senior Capstone Experience projects, research for course credit or shadowing opportunties. If you are excited to learn more about the research and techniques utilized in my lab, please send me an email or stop by my office. 

For a list of current and former lab members, please click here.

Publications

Lipchock JM and Loria JP. “Nanometer propagation of millisecond motions in V-type allostery.” Structure. 2010, 18: 1596-1607.

Lipchock JM and Loria JP. “Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) form Thermotoga maritima.” J. Biomolec. NMR, 2009, 45: 73-84.

Lipchock JM and Loria JP. “Monitoring molecular interactions by NMR.” Methods in Mol. Biol., 2009, 490: 115-134.

Lipchock JM and Loria JP “1H, 15N, 13C resonance assignment of imidazole glycerol phosphate (IGP) synthase protein HisF from Thermotoga maritima.” Biomolec. NMR Assignments, 2008, 2: 219-221.

Kroeger Smith MB, Hose MD, Hawkins A, Lipchock J, Farnsworth DW, Rizzo RC, Tirado-Rives J, Arnold E, Zhang W, Hughes SH, Jorgensen WL, Michejda CJ, Smith RH Jr. “Molecular modeling calculations of HIV-1 reverse transcriptase non-nucleoside inhibitors: correlation of binding energy with biological activity for novel 2-aryl-substituted benzimidazole analogs.” J. Med. Chem., 2003, 46: 1940-1947.