Abstract
The interaction of the cAMP receptor protein (CRP) of Escherichia coli with a synthetic DNA undecamer (11mer) comprising a portion of the specific target site in the gal operon and containing 8 basepairs out of the 10 basepair concensus making up specific CRP sites, has been studied by circular dichroism spectroscopy. The binding constants for the interaction of CRP with the 11mer in the presence and absence of cAMP have been determined, and it is shown that CRP, both in the presence and absence of cAMP, induces a BC transition in the conformation of the 11mer.
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