Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
| Autor: | Jean-Paul Mornon, Christine Gaboriaud, T. Benchetrit, V. Bissery |
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| Rok vydání: | 1987 |
| Předmět: |
Protein sequence comparison
Protein Conformation Conformation homology Biophysics Computational biology Rhodanese Biology Biochemistry Protein structure Azurin Structural Biology Sequence Homology Nucleic Acid Methods Genetics Cluster (physics) Animals Humans Amino Acid Sequence Plastocyanin Molecular Biology Peptide sequence Protein primary structure Cell Biology Protein structure prediction Thiosulfate Sulfurtransferase Globins Rats Leghemoglobin |
| Zdroj: | FEBS Letters. 224:149-155 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(87)80439-8 |
| Popis: | A new method for comparing and aligning protein sequences is described. This method, hydrophobic cluster analysis (HCA), relies upon a two-dimensional (2D) representation of the sequences. Hydrophobic clusters are determined in this 2D pattern and then used for the sequence comparisons. The method does not require powerful computer resources and can deal with distantly related proteins, even if no 3D data are available. This is illustrated in the present report by a comparison of human haemoglobin with leghaemoglobin, a comparison of the two domains of liver rhodanese (thiosulphate sulphurtransferase) and a comparison of plastocyanin and azurin. |
| Databáze: | OpenAIRE |
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