2011
DOI: 10.1111/j.1742-4658.2011.08198.x
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Solution parameters modulating DNA binding specificity of the restriction endonuclease EcoRV

Abstract: Summary The DNA binding stringency of restriction endonucleases is crucial for their proper function. The x-ray structures of the specific and non-cognate complexes of the restriction nuclease EcoRV are considerably different suggesting significant differences in the hydration and binding free energies. Nonetheless, the majority of studies performed at pH 7.5, optimal for enzymatic activity, have found less than a 10-fold difference between EcoRV binding constants to the specific and nonspecific sequences in t… Show more

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Cited by 15 publications
(39 citation statements)
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“…This large increase is because the specific EcoRV-DNA complex sequesters some 120 fewer water molecules from glycine betaine than the nonspecific complex. Other solutes, triethylene glycol, TMAO, and methyl glucoside influence the EcoRV binding specificity in a similar way (15) confirming that solutes act osmotically, i.e. by changing water activity.…”
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confidence: 68%
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“…This large increase is because the specific EcoRV-DNA complex sequesters some 120 fewer water molecules from glycine betaine than the nonspecific complex. Other solutes, triethylene glycol, TMAO, and methyl glucoside influence the EcoRV binding specificity in a similar way (15) confirming that solutes act osmotically, i.e. by changing water activity.…”
mentioning
confidence: 68%
“…In the binding reaction, EcoRV is incubated in the absence of divalent cofactor with a 310 bp DNA fragment containing a single EcoRV specific site for a long enough times to ensure that all protein is specifically bound to the DNA fragment (15). Typically the enzyme to recognition site ratio is 0.5–0.6.…”
Section: Resultsmentioning
confidence: 99%
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