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Actin Hydrophobic Loop (262-274) and Filament Nucleation and Elongation
The importance of actin hydrophobic loop 262-274 dynamics to actin polymerization and filament stability has been shown recently using a yeast actin mutant, L180C/L269C/C374A, in which the hydrophobic loop could be locked in a “parked” conformation by a disulfide bond between C180 and C269. Such a c...
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| Autors principals: | , , , , , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
2007
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4022318/ https://ncbi.nlm.nih.gov/pubmed/18037437 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2007.10.076 |
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