Abstract
Protein 3-D structures are more functionally conserved than sequence and this claims the need of developing a computational tool for accurate protein structure comparison at the global and local levels. We have developed a novel geometry-based method for protein 3-D structure comparison using the concept of Triangular Spatial Relationship (TSR).
Highlights
Protein 3-D structures are more functionally conserved than sequence and this claims the need of developing a computational tool for accurate protein structure comparison at the global and local levels
We have developed a novel geometry-based method for protein 3-D structure comparison using the concept of Triangular Spatial Relationship (TSR)
It is well known that hydrophobic amino acids are most likely found in the core of globular proteins
Summary
Protein 3-D structures are more functionally conserved than sequence and this claims the need of developing a computational tool for accurate protein structure comparison at the global and local levels. We have developed a novel geometry-based method for protein 3-D structure comparison using the concept of Triangular Spatial Relationship (TSR). The analysis of keys provides a deeper insight into structure and function relations of the proteins. 100% of serine proteases, kinases, and phosphatases have one of these two keys, and these two keys have their specific Theta and MaxDist values.
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