Om Prakash, Ph.D.
Director of NMR Facility
Graduate Admissions Chair Undergraduate Advisor
Areas of specialty
- Structural characterization and molecular recognition using nuclear magnetic resonance (NMR) and computer aided molecular design (CAMD)
Our laboratory uses state-of-the-art multidimensional NMR spectroscopy along with computer aided molecular modeling to solve structural and dynamics problems in molecular pharmacology, rational drug designing, protein folding and solution phase biostructure. We are interested in utilizing structure of peptides, proteins, enzymes, receptors and acceptors as templates in drug designing. We are also interested in developing programs and routines for computer aided structure and conformation elucidation. Once an accurate model is determined, we use it as a template for design of appropriate constrained peptide ligands.
In summary, the integration of above mentioned knowledge such as structure-function and molecular recognition may play a key role for the successful design of pharmaceuticals in the future. Furthermore, these studies can guide the design of future experiments, particularly that employing recombinant DNA technology to create new protein structures useful in developing resistance to insects and diseases in plants and animals.
Takahashi, D., Hiromasa, Y., Kim, Y., Anbanandam, A., Yao, X., Chang, K., and Prakash, O. (2013) Structural and dynamics characterization of norovirus protease. Protein science, 22:347-357.
Huang, H., Herrera, A., Luo, Z., Sun, XS., and Prakash, O. (2012) Structural transformation and physical properties of a hydrogel forming peptide studied by NMR, TEM and dynamic rheomter. Biophysical Journal, 103:979-988.
Takahashi, D., Kim, Y., Chang, K-O., Anbanandam, A., and Prakash, O. (2012) Backbone and side-chain 1H, 15N, and 13C resonance assignments of Norwalk virus protease. Biomol. NMR Assign., 6:19-21.
Bai, Y., Shi, Y-C., Herrera, AI., and Prakash, O. (2011) Study of octenyl succinic anhydride modified waxy maize starch by nuclear magnetic resonance spectroscopy. Carbohydrate Polymers, 83:407-413.
Shera, JN., Takahashi, D., Herrera, A., Prakash, O., and Sun, X. (2010) Morphology and Structural Properties of pH-Responsive Amphiphilic Peptides. Journal of Nanoscience and Nanotechnology, 10:7981-7987.
Takahashi, D., Shukla, SK., Prakash, O., and Zhang, G. (2010) Structural Determinants of Host Defense Peptides for Antimicrobial Activity and Target Cell Selectivity. Biochimie, 92:1236-1241.
Sang, Y., Seib, PA., Herrera, AI., Prakash, O., and Shi, Y-C. (2010) Effects of Alkaline Treatment on Structure of Phosphorylated Wheat Starch and its Digestibility. Food Chemistry, 118:323-327.
Herrera, A., Al-Rawi, A., Cook, GA., Gao, J., Iwamoto, T., Prakash, O., Tomich, JM., and Chen, J. (2010) Introduction of a C-Terminal Tryptophan in a Pore-Forming Peptide: A Structure/Activity Study. Proteins, 78:2238-2250.
Zhang, G., and Prakash, O. (2010) NMR Insights into Structure-Activity Relationships of Fowlicidins, Chapter 10 in Future Directions of NMR edited by C. L. Khetrapal, Anil Kumar and K.V. Ramanathan, published by Springer-Verlag-India, ISBN: 8184899947.
Lauer, J., Banerjee, D., Shanks, D., Dai, H., Gong, Y-X., Prakash, O., and Takemoto, DJ. (2010) NMR/Function Relationship of Peptide Corresponding to the C1B1 region of PKCγ. Protein & Peptide Letters, 17:1-10.
Xiao, Y., Herrera, A., Soulages, JL., Bommineni, YR., Prakash, O., and Zhang, G. (2009) The central kink region of an α-helical host defense peptide, is critically involved in bacterial killing and endotoxin neutralization. Journal of Innate Immunity, 1:256-280.