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Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands
SecB, a remarkable chaperone involved in protein export, binds diverse ligands rapidly with high affinity and low specificity. Site-directed spin labeling and electron paramagnetic resonance spectroscopy were used to investigate the surface of interaction on the export chaperone SecB. We examined Se...
Tallennettuna:
| Päätekijät: | , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Wiley Subscription Services, Inc., A Wiley Company
2009
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2777361/ https://ncbi.nlm.nih.gov/pubmed/19569227 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.197 |
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