Title : Effect of mutations at the monomer-monomer interface of cAMP receptor protein on specific DNA binding.

Pub. Date : 1999 Mar 12

PMID : 10066748






6 Functional Relationships(s)
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1 The binding reactions of the DNA duplexes to the fully cNMP-ligated CRP-mutant complexes were endothermic with binding constants as high as 6.6 +/- 1.1 x 10(6) M-1 (conDNA.CRP(cAMP)2). Cyclic AMP C-reactive protein Homo sapiens
2 The binding reactions of the DNA duplexes to the fully cNMP-ligated CRP-mutant complexes were endothermic with binding constants as high as 6.6 +/- 1.1 x 10(6) M-1 (conDNA.CRP(cAMP)2). Cyclic AMP C-reactive protein Homo sapiens
3 ConDNA binding to the unligated T127L and CRP* mutants was observed as well as conDNA and lacDNA binding to CRP with cAMP bound to only one monomer. Cyclic AMP C-reactive protein Homo sapiens
4 The reduction of the binding constants with increase in KCl concentration indicated the formation of two ion pairs for the cAMP-ligated CRP and S128A complexes and four ion pairs for the cAMP-ligated T127L and CRP* complexes. Cyclic AMP C-reactive protein Homo sapiens
5 The reduction of the binding constants with increase in KCl concentration indicated the formation of two ion pairs for the cAMP-ligated CRP and S128A complexes and four ion pairs for the cAMP-ligated T127L and CRP* complexes. Cyclic AMP C-reactive protein Homo sapiens
6 Small angle neutron scattering measurements on the lacDNA.CRP(cAMP)2 complex in D2O/H2O mixtures show that the DNA is bent around the cAMP-ligated protein in solution. Cyclic AMP C-reactive protein Homo sapiens