期刊论文详细信息
| FEBS Letters | |
| Relative‐residue surface‐accessibility patterns reveal myoglobin and catalase similarity | |
| Osguthorpe, D.J.1  Cockcroft, V.B.1  | |
| [1] Molecular Graphics Unit, Bath University, Bath BA2 7AY, UK | |
| 关键词: Relative-residue surface-accessibility pattern; Non-homologous similarity; Myoglobin; Catalase; | |
| DOI : 10.1016/0014-5793(91)81173-6 | |
| 学科分类:生物化学/生物物理 | |
| 来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201912020295613ZK.pdf | 388KB |
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