Department of Chemistry
Loyola University New Orleans

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   William Walkenhorst, Ph.D.

   Associate Professor of Chemistry
   Phone: (504)865-3270

   Office: Monroe Hall 211

   Lab: Monroe Hall 226

   email: walken@loyno.edu
   Research Group Website

 

Education

Ph. D., Biochemistry, University of Wisconsin-Madison, 1993

Thesis Advisor: John L. Markley

Thesis:  Structural Investigations of Ovomucoid Third Domains by NMR Methods               

B. S., Chemistry, Bradley University, Peoria, IL, 1983

                         

Honors & Fellowships

NIH NRSA Postdoctoral Fellowship, Fox Chase Cancer Center, July 1994 to July 1996, Sponsor: Dr. Heinrich Roder 

NIH Molecular Biology Training Grant Postdoctoral Fellowship, Fox Chase Cancer Center, 1993-94

Amoco Fellowship, 1990-91, Department of Biochemistry, University of Wisconsin-Madison.

Research Interests

My research involves studying the structure, function, and stability of peptides and proteins in solution.  I use chemical, biological, and instrumental techniques to study several classes of proteins. My most recent project involves studying the effectiveness of membrane active peptide antibiotics under various solution conditions.   I conduct research with both chemistry and biology undergraduate students.  I am a founding member of the New Orleans Protein Folding Intergroup (NOProFIG) which began in January 1999 and meets every two weeks to discuss research results of local researchers in related fields (http://www.tulane.edu/~NOProFIG/).   

Representative Publications

1. Walkenhorst, W.F., Edwards, J.A., Markley, J.L., and Roder, H. “Early Formation of a Beta Hairpin during Folding of Staphylococcal Nuclease H124L as Detected by Pulsed Hydrogen Exchange”,  Protein Science  11:82-91 (2002).

2. Bishop, C.M., Walkenhorst, W.F., and Wimley, W.C.  “Folding of Beta-Sheets in Membranes: Specificity and Promiscuity in Peptide Model Systems”,  J. Mol. Biol.  309: 975-988 (2001).

 3. Green, G.R., Ferlita, R.R., Walkenhorst, W.F., and Poccia, D.L.   “Linker DNA Destabilizes Condensed Chromatin”,   J. Biochem. Cell Biol.  79: 349-363  (2001).

 4. Walkenhorst, W.F., Green S.M., and Roder, H., (1997) “Kinetic Evidence for Folding and Unfolding Intermediates in Staphylococcal Nuclease”, Biochemistry 36, 5795-5805.

5. Hinck, A.P., Walkenhorst, W.F., Truckses, D.M., and Markley, J.L.  “NMR and Mutagenesis Investigations of a Model Cis:Trans Peptide Isomerization Reaction: Xaa116-Pro117 of Staphylococcal Nuclease and its Role in Protein Stability and Folding”, (review in Biological NMR Spectroscopy, Oxford University Press, 133-160 (1996). 

 6. Pinkerton, T.C., Howe, J.W., Ulrich, E.L., Comiskey, J.P., Haginaka, J., Murashima, T.,

Walkenhorst, W.F., Westler, W.M., and Markley, J.L.  “Protein Binding Chiral Discrimination of HPLC Stationary Phases made with Whole, Fragmented, and Third Domain of Turkey Ovomucoid”,  Anal. Chem. 67, 2354-2367 (1995).

7. Walkenhorst, W.F., Krezel, A.M., Rhyu, G.I., and Markley, J.L. "Solution Structure of  Reactive-Site Hydrolyzed Turkey Ovomucoid Third Domain by Nuclear Magnetic Resonance and Distance Geometry Methods",  J. Mol. Biol. 242, 215-230 (1994).

8. Hinck, A.P., Walkenhorst, W.F., Westler, W.M., Choe, S., and Markley, J.L.  "Overexpression

and Purification of Avian Ovomucoid Third Domains in Escherichia coli",  Protein Engineering 6, 221-227 (1993).

9. McWherter, C.A., Walkenhorst, W.F., Campbell, E.J., and Glover, G.I. "Novel Inhibitors of

Human Leukocyte Elastase and Cathepsin G.  Sequence Variants of Squash Seed Protease Inhibitor with Altered Protease Selectivity",  Biochemistry 28, 5708-5714  (1989).