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Posters
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Superimposition of Protein Structures through weighted RMSD
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Di Wu1 and Brady Garabato2
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The biological functions of proteins are highly correlated to their motions and
flexibilities that can regulate activities, such as protein-protein interactions
and enzymes and catalyzers in biochemical reactions. A protein can change
its conformation over time due to its functions in biological systems, such as ion
channels in membrane proteins, a protein switch for turning on or off the activity,
and receptors in cell signaling. An overlay of different conformations of
a protein provides vision check and quantitative analysis to comparison of protein
structures and identifications of mobile regions of a protein, and hence has been
widely applied. In this work, a novel method of superimposing protein structures
is investigated. The results show that protein domains and motions have been
successfully identified and superimposition of protein structures by using this
method provides higher correlation with protein dynamics.
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1Department of Mathematics, Western Kentucky University Bowling Green,
KY
2Department of Chemistry, Western Kentucky University Bowling Green,
KY
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