Relative‐residue surface‐accessibility patterns reveal myoglobin and catalase similarity
A novel sliding‐window search method using relative‐residue surface‐accessibility patterns identified extensive, but unsuspected, structural similarity over a 3‐helix region in the C‐terminus of the evolutionarily unrelated proteins sperm‐whale myoglobin and beef liver catalase. This clear example o...
| Published in: | FEBS Letters |
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| Main Authors: | , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
1991
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1016/0014-5793(91)81173-6 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793%2891%2981173-6 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2F0014-5793(91)81173-6 https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2891%2981173-6 |
| Summary: | A novel sliding‐window search method using relative‐residue surface‐accessibility patterns identified extensive, but unsuspected, structural similarity over a 3‐helix region in the C‐terminus of the evolutionarily unrelated proteins sperm‐whale myoglobin and beef liver catalase. This clear example of structural similarity between non‐homologous proteins highlights the importance of relative‐residue surface‐accessibility patterns in understanding the local folded structure in proteins. |
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