Mark J. Snider

Mark J. Snider, Associate Professor of Chemistry, is a native of Ohio. He received his B.A. in Chemistry at Capital University in 1997 and his Ph.D. in Biochemistry with emphasis in Biophysics with Richard Wolfenden at the University of North Carolina at Chapel Hill in 2001. He joined the chemistry faculty in the summer of 2001, starting at the College in a unique half-time teaching and half-time post-doctoral research position under the mentorship of Professor (Emeritus) Charles Borders. During the 2007-2008 academic year, Mark took a research leave to work with Tadhg Begley in the Department of Chemistry & Chemical Biology at Cornell University.

Trained as a physical biochemist, Mark's current research interests include: Kinetic and mechanistic studies of uncatalyzed and enzyme-catalyzed creatine hydrolysis; Genes and mechanistic enzymology of NAD metabolism; Comparative structure-function investigations of rabbit muscle creatine kinase and C. elegans arginine kinases; and Determining function of proteins.

Mark teaches a variety of courses within the Department, including the Introductory College Chemistry Courses, Organic Chemistry, Biochemistry, Biophysical Chemistry, Techniques in Biochemistry & Molecular Biology, Introduction to Independent Study, as well as First Year Seminar in Critical Inquiry. He enjoys the occasional opportunity for biking, hiking, gardening, or to play the violin.

Curriculum Vitae

Recent Publications:

A. Hazra, M. J. Snider, A. Chatterjee, D. Chatterjee, J. W. Hanes, D. G. Hilmey, K. Krishnamoorthy, K. M. Mccullock, S. O'Leary, J. M. Sanders, M. J. Waitner, and T. P. Begley (2008) Coenzyme and prosthetic group biosynthesis; Encyclopedia of Microbiology - in press.

L. D. Andrews*, J. Graham*, M. J. Snider, D. Fraga. (2008) Characterization of a novel bacterial arginine kinase from Desulfotelea psychrophilia - Comparative Physiology and Biochemistry; Part B: Biochemistry & Molecular Biology 150: 312-319.

M. J. Jourden*, C. N. Clarke*, A. K. Palmer*, E. J. Barth*, R. C. Prada*, R. N. Hale*, D. Fraga, M. J. Snider, P. L. Edmiston (2007) Changing the substrate specificity of creatine kinase from creatine to glycocyamine: evidence for a highly evolved active site. Biochimica et Biophysica Acta - Proteins and Proteomics 1774: 1519-1527.

M. J. Jourden, M. J. Thomenius, P. R. Geiss, L. A. Horst, M. M. Barty, G. B. Mulligan, R. M. Almeida, B. A. Kersteen, N. R. Myers, M. J. Snider, C. L. Borders, Jr., P. L. Edmiston (2005) Transition state stabilization by six arginines clustered in the active site of creatine kinase. Biochimica et Biophysica Acta - Proteins and Proteomics 1751: 178-183.

C. H. Borchers, V. E. Marquez, G. K. Gottfried, S. E. Short, M. J. Snider, P. Speir and R. Wolfenden (2004) Fourier transform ion cyclotron resonance mass spectrometry reveals the presence of a water molecule in an enzyme-transition state analogue complex. Proceedings of the National Academy of Sciences - USA 101: 15341-15345.

M. Snider, B. Temple and R. Wolfenden (2004) The path to the transition state in enzyme reactions: a survey of catalytic efficiencies. Journal of Physical Organic Chemistry 17: 586-591.

R. Wolfenden and M. J. Snider (2001) The Depth of Chemical Time and the Power of Enzymes as Catalysts. Accounts of Chemical Research 34, 938-945.

Recent Presetations at Professional Meetings:
(*College of Wooster undergraduate; presenter)

M. P. McGinley*, D. Fraga and M. Snider (2008) Evolution of cooperativity in the phosphagen kinase family. FASEB J. 22: 1004.3

V. M. Andrus*, D. Thomas*, T. Meulia, M. Snider, and D. Fraga (2008) Characterization of the arginine kinase family of Caenorhabditis elegans. FASEB J. 22: 1004.4

C. Clarke*, and M. J. Snider (2007) Rate of spontaneous hydrolysis of creatine to estimate the catatlyic proficiency of creatine amidinohydrolase. FASEB J. 21: 650.5

P. S. Agidi*, M. J. Snider; Experimental Biology 2007 (ASBMB National Conference), Washington D.C. April 2007.

C. Clarke*, M. J. Snider; Catalytic proficiency of creatine amidinohydrolase. Experimental Biology 2007 (ASBMB National Conference), Washington D.C. April 2007.

D. H. Thomas*, M. J. Snider; Experimental Biology 2007 (ASBMB National Conference), Washington D.C. April 2007.

J. Graham*, and L. Stetzik*, M. J. Snider; Investigating cooperative ligand binding by rabbit muscle creatine kinase using isothermal titration calorimetry. Midwest Enzyme Chemistry Conference, Northwestern University, Il. September 2006.

Mark J. Snider, I. Lee, I. Eccles-James*, J. Anquandah*, J. Graham*, and L. Stetzik*; Dimerization enhances rate of product release in phosphagen kinase family. Gordon Research Conference on Enzymes, Coenzymes and Metabolic Pathways, University of New England, ME; July 2006.

J. Anquandah*, I. Eccles-James*, and M. J. Snider; A mechanistic role for protein oligomerization in the phosphagen kinase family. Experimental Biology 2006 (ASBMB National Conference), San Francisco, CA; April 2006.

E. E. Gustely* and M. J. Snider; Analysis of the role of His232 in the mechanism of Ps. putida creatinase. Experimental Biology 2006 (ASBMB National Conference), San Francisco, CA; April 2006.

H.-D. Nguyen* and M. J. Snider; Is the ATP analogue adenosine-5'-sulfatopyrophosphate an alternative substrate or inhibitor of creatine kinase? Experimental Biology 2006 (ASBMB National Conference), San Francisco, CA; April 2006.

B. D. Pipitone* and M. J. Snider; Determining the subcellular localization of a novel arginine kinase in C. elegans. Experimental Biology 2006 (ASBMB National Conference), San Francisco, CA; April 2006.

L. A. Horst*, Z.-M. Tun*, J. B. Tout*, M. J. Jourden*, J. A. Bayuk*, J. M. Shear*, M. J. Snider; Thermodynamic analysis of substrate binding and activation by rabbit muscle creatine kinase. 19th Enzyme Mechanisms Conference, Pacific Grove, CA; January 2005.

Recent Invited Lectures

Negative cooperativity in transition state binding enhances rate of product release in phosphagen kinases; 40th Central Regional Meeting of the American Chemical Society Ð Symposium in Honor of Professor Ming-Daw Tsai; Columbus, OH; June 2008.

Thermodynamics and cooperativity of transition state binding by creatine kinase; Department of Chemistry; Ithaca College, Ithaca, NY; March 2008.

Thermodynamics of enzyme action; Department of Biological and Chemical Sciences; Wells College, Aurora, NY; February 2008.

The importance of institutional, disciplinary, and interdisciplinary definitions of scholarship; The Student as Scholar: Undergraduate Research and Creative Practice; AAC&U Conference; Long Beach, CA; April 2007.

Thermodynamics and cooperativity of transition state binding by phosphagen kinases; Biological Chemistry Division Seminar, Department of Chemistry, The Ohio State University; January 2007.

Structure-function analyses of the mechanisms of phosphagen kinases; Department of Biochemistry & Molecular Biology, Pennsylvania State University; October 2006.

Structure-function analyses of the mechanisms of phosphagen kinases; Department of Chemistry, The University of Akron; March 2006.

Kinetic and thermodynamic explorations of the mechanism of creatine kinase; T. Begley Laboratory, Department of Chemistry and Chemical Biology, Cornell University; February 2006.

Kinetic and thermodynamic explorations of the mechanism of creatine kinase; Department of Chemistry, Michigan State University; July 2005.

Getting started in teaching and research at a primarily undergraduate institution, Program in Molecular & Cellular Biophysics, Department of Biochemistry & Biophysics, University of North Carolina at Chapel Hill; March 2005.

Externally-Funded Research Grants

2008-2011: National Science Foundation: Major Research Instrumentation Program: Acquisition of an LC/MS/MS to Enhance Undergraduate Research and Teaching, by Melissa Schultz (PI), Paul Edmiston (Co-PI) and Mark Snider (Co-PI); $226,115

2006-2009: National Science Foundation: Major Research Instrumentation Program; Acquisition of an Isothermal Titration Calorimeter by Paul Bonvallet (PI), Don Jacobs (Co-PI), and Mark Snider (Co-PI); $91,090

2004-2007: National Science Foundation; Metabolic Biochemistry Program; Comparative Structure - Function Analysis of Phosphagen Kinases by Mark Snider (PI), Paul Edmiston (Co-PI), and Dean Fraga (Co-PI); $320,307