3 D MODEL GENERATIONS OF BACTERIAL TOXINS
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Date
2011
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Abstract
Proteins are key biological molecules with diverse functions. They take part in maintaining the
structural integrity of the cell, transport and storage of small molecules, catalysis, regulation,
signaling and the immune system. Linear protein molecules fold up into specific three-dimensional
structures, and their functional properties depend intricately upon their structures. It is a great
challenge for nowadays biologists to predict the three- dimensional structure of a protein from its
linear sequence. Proteins, amino acid chains, are made up from 20 different amino acids that are
folded into unique three-dimensional protein structures. These structures are determined by their
sequence of amino acids. Bacterial toxins continue to impose a major threat to public health
worldwide in the 21st century. Information on bacterial toxin is important for molecular cell
biology, proteomics and system biology and drug discovery. Intensified studies on bacterial toxins
have greatly expanded our knowledge about the mechanisms of the disease processes at the molecular
level over the last decades. Thus the ultimate goal of protein modeling of bacteria toxins is to
predict a structure from its sequence with accuracy. These would allow users to safely use rapidly
generated Insilco protein models in all the contexts where today only experimental structures
provide a solid basis: structure-based drug design, analysis of protein function, interactions,
antigenic behavior, and rational design of proteins with increased stability or novel functions.
These models are the only way to obtain structural information if experimental techniques fail. To
provide the structural information of bacteria toxins that are not present in PDB,
prediction of those protein structures becomes necessary. This report contains 30 three dimensional protein models of bacteria toxins. Using these modeled structures; one can easily get some bit of information.