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Research/Teaching Interests

• Protein folding. Understanding the mechanism by which proteins acquire their precisely folded three-dimensional structures remains one of the most important challenges of structural biology. To solve this complex problem, a variety of experimental techniques as well as computational methods of analysis are used to probe the role of different interactions in protein folding and protein interactions with ligands. Answers to the protein-folding problem play a key role in designing proteins with new functional properties and improved methods for protein structure prediction. Moreover, a thorough understanding of the principles that govern folding of proteins in vitro is a prerequisite for elucidating protein folding in the cell, which has far-reaching biological and medical implications.
  
  
• Topoisomerase I. The replication, transcription, recombination, and repair of DNA is modulated by enzymes, among these enzymes is Topoisomerase. Topoisomerase can modulate topological structure of DNA and play an important role in the many aspects of chromosome function. Recently, Topoisomerase I has been identified as an important pharmacological target for some anti-cancer drugs. Studies on the mechanism of Topoisomerase I can provide insight into new chemotherapeutics.
  
  
• Androgen Receptor. In mammals, natural testosterones play a critical role in the normal development and function of the sex organs in males and the maintainence of spermatogenesis. The actions of androgens are mediated by the androgen receptor (AR). These receptors have distinct domains for DNA binding, ligand binding, and transcriptional activation. When androgens bind to the androgen receptor, a change takes place causing dissociation of the androgen receptor/DNA complex and results in transcriptional activation. Androgen activation is stongly linked to prostate cancer. The unique requirement of androgens to maintain the growth of the tumor and evade apoptosis is the basis for androgen blocking therapies. Because androgen bound to the androgen receptor is completely enveloped by protein, it is thought that the process of ligand binding or unbinding must involve a significant conformational change. Probing the mechanism of ligand binding and release can have far reaching consequences toward drug design that targets certain types of prostate cancer.

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Selected Publications/Presentations

Publications

• Salopek-Sondi, B., Skeels, M.C., Swartz, D. and Luck, L.A. (2003) Insight into the Stability of the Hydrophobic Amino Acid Binding Proteins of E.coli: Assessing the Proteins for use as Biosensors. Proteins: Structure, Function and Genetics. 53, (2) 273-281.
  
  
• Salopek-Sondi, B., Vaughn, M.D., Skeels, M.C., Honek, J.F. and Luck, L.A. (2003) 19F NMR Studies of the Leucine-Isoleucine-Valine Binding Protein: Evidence That a Closed Conformation Exists in Solution. Journal of Biomolecular Structure & Dynamics 21, 235-246.
  
  
• Skeels, M.C., Sondi, B.S., and Luck, L.A. (1999) 19F NMR Study of the Binding of Fluorinated Diethylstilbestrol to the Human Estrogen Receptor. Protein and Peptide Letters 6 149-154.

Poster Presentations

• Beckman, S., Smith-Packard, B. Peploski, J. and Skeels, M. 2003. Refining a DNA Fingerprinting procedure for use in the Freshman Forensics Lab. 4th Annual Sure, Clarkson University, Potsdam, NY.
  
  
• McPherson, B., Felton, D., Rossner, A., and Skeels, M. 2003. Investigation of Aireborne Fungal Spores using PCR-based methods. 4th Annual Sure. Clarkson University, Potsdam, NY.
  
  
• Luck, L.A., Barse, J.L Skeels, M., Sondi, B., Luck, A.M., and Peck, C. 2000. 19F NMR Studies of the Estrogen Receptor, Breast Cancer Research Program, Department of Defense, U.S. Army Research and Material Command, Atlanta, GA.
  
  
• Mabb, A., Skeels, M., and Luck, L.A. 2000. Production of the Recombinant Human Estrogen Receptor for Determination of Xeno-Estrogens Using a Piezoelectric Sensor, 2nd Annual Sure, Clarkson University, Potsdam, NY.
  
  
• Luck, L.A., Skeels, M.C., Sondi, B.S., Marin, V., Johnson, C., and Poteralski, J. 1999. 19F NMR Studies of the Estrogen Receptor, Northeast Regional Meeting of the ACS, Potsdam, NY.

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