Nucleases micrococcal, active site

This system has also been shown to be dependent on the secondary structure of DNA, the A, B, and Z forms reacting at different rates [150]. The likely explanation is that the faster reacting B DNA forms a more stable complex with the catalyst. This artificial DNase activity has also been compared with cleavage by micrococcal nuclease, and shown to recognize the same sites but not all those cleaved by DNase 1, again implying some local conformational preferences [151]. Chromatin structure has also been probed [152]. 

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