Abstract
The accuracy of protein sequence alignment obtained by applying a commonly used global sequence comparison algorithm is assessed. Alignments based on the superposition of the three-dimensional structures are used as a standard for testing the automatic, sequence-based methods. Alignments obtained from the global comparison of five pairs of homologous protein sequences studied gave 54% agreement overall for residues in secondary structures. The inclusion of information about the secondary structure of one of the proteins in order to limit the number of gaps inserted in regions of secondary structure, improved this figure to 68%. A similarity score of greater than six standard deviation units suggests that an alignment which is greater than 75% correct within secondary structural regions can be obtained automatically for the pair of sequences.
| Original language | English |
|---|---|
| Pages (from-to) | 89-94 |
| Number of pages | 6 |
| Journal | Protein Science |
| Volume | 1 |
| Issue number | 2 |
| Publication status | Published - 1 Feb 1987 |
Keywords
- Algorithms
- Amino Acid Sequence
- Molecular Sequence Data
- Protein Conformation
- Protein Engineering