The helicity of DNA in complexes with RecA protein
✍ Scribed by Stasiak, Andrzej; Di Capua, Elisabeth
- Book ID
- 109727517
- Publisher
- Nature Publishing Group
- Year
- 1982
- Tongue
- English
- Weight
- 321 KB
- Volume
- 299
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/299185a0
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## Abstract In an attempt to understand the role of ATP as a cofactor at the interaction of the RecA protein with DNA, we have studied the orientation geometries of the cofactor analogs adenosine 5′‐__O__‐(3‐thiotriphosphate) (ATPγS) and guanosine 5′‐__O__‐(3‐thiotriphosphate) (GTPγS) in RecA‐DNA c
Double-helical metal complexes, the helicates H2-Hs, were found to bind to double-helical DNA by spectroscopic, DNA-melting, and electrophoretic-mobility measurements. The helicates also inhibited the cleavage of DNA by two restriction enzymes, SspI and EcoRV, a property which agrees with the bindin