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Structural and Functional Characterization of RecG Helicase under Dilute and Molecular Crowding Conditions
In an ATP-dependent reaction, the Escherichia coli RecG helicase unwinds DNA junctions in vitro. We present evidence of a unique protein conformational change in the RecG helicase from an α-helix to a β-strand upon an ATP binding under dilute conditions using circular dichroism (CD) spectroscopy. In...
Tallennettuna:
| Päätekijät: | , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Hindawi Publishing Corporation
2012
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3420092/ https://ncbi.nlm.nih.gov/pubmed/22919464 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1155/2012/392039 |
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