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| + | {{tag>other}} | ||
| + | ====== SSAP ======= | ||
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| + | Full name: __Secondary Structure Alignment Program.__ | ||
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| + | This secondary structure alignment program uses dynamic programming to align proteins by matching vectors between residues. For each residue in a protein, a local | ||
| + | structural environment is defined by a set of inter-atomic vectors. The method | ||
| + | matches residues by comparing these structural environments. An important aspect | ||
| + | of these environments is that because they are defined independently for each | ||
| + | residue, they are rotationally invariant, making their comparison insensitive | ||
| + | to the displacement of substructures. This method also allows other residue | ||
| + | properties to be included in the comparison, including solvent accessible | ||
| + | area and torsional angles (corresponding to degree of burial and secondary | ||
| + | structure), thus improving the alignment of remote protein structures. An important | ||
| + | advantage of this method is that it is completely automatic. This algorithm is used to | ||
| + | cluster structurally similar proteins in the CATH system. | ||
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| + | ===== References ===== | ||
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| + | {{pubmed>long:8411157}} | ||
| + | {{pubmed>long:2769748}} | ||
| + | {{pubmed>long:2748567}} | ||
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