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A conformational study of a glutamine- and proline-rich cereal seed protein, C hordein.
A combination of c.d. spectroscopy and computer prediction is used to show that C hordein has an unusual secondary structure with an absence of alpha-helix and beta-sheet, but the presence of regularly repeated beta-turns. This is associated with a repetitive primary structure based mainly on blocks...
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| Autors principals: | , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
1985
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1144744/ https://ncbi.nlm.nih.gov/pubmed/3994673 |
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