Three‐dimensional, sequence order‐independent structural comparison of a serine protease against the crystallographic database reveals active site similarities: Potential implications to evolution and to protein folding
We have recently developed a fast approach to comparisons of 3‐dimensional structures. Our method is unique, treating protein structures as collections of unconnected points (atoms) in space. It is completely independent of the amino acid sequence order. It is unconstrained by insertions, deletions,...
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Veröffentlicht in: | Protein science 1994-05, Vol.3 (5), p.769-778 |
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