University of Maryland

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University of Maryland

Proteins form the basis for life because they regulate the cellular machinery defining all known organisms. Incredibly complex, protein molecules fold into unique three-dimensional shapes that give them their chemical properties in cells. Determining these structures is extremely important for our understanding of what proteins do and how they do it. For instance, the p53 "tumor suppressor" protein is known to be involved in important metabolic pathways for the body's destruction of precancerous cells. Understanding the structure of proteins like p53 can be crucial to discovering new cancer treatments, and in finding ways of preventing cancer altogether.

Although much is known about many important human proteins, scientists are continuing to learn about the composition, formation, and structure of proteins. Current methods of determining protein structure are time-consuming, expensive, and sometimes entirely impractical. Parabon is working with a team of researchers from the University of Maryland to simulate how proteins fold and to better understand the process. The power of the Frontier platform enables research into new methods to simulate the folding of proteins and further this critical research.

1PDB ID: 1HS5 T. S. Davison, X. Nie, W. Ma, Y. Li, C. Kay, S. Benchimol, C. H. Arrowsmith; NMR Solution Structure of Designed P53 Dimer; To be Published (2001)

2H.M.Berman, J.Westbrook, Z.Feng, G.Gilliland, T.N.Bhat, H.Weissig, I.N.Shindyalov, P.E.Bourne; The Protein Data Bank Nucleic Acids Research, 28 pp. 235-242 (2000) http://www.rcsb.org/pdb/.

 

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