| Value |
2.8e+7
Sec^-1×M^-1
Range: Table - link Sec^-1×M^-1
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Nelson HC, Sauer RT. Lambda repressor mutations that increase the affinity and specificity of operator binding.Cell. 1985 Sep42(2):549-58. p.552 table 3PubMed ID3161621
|
| Method |
Researchers describe ? repressor mutants that bind operator
DNA more tightly, and in some cases more specifically,
than wild-type repressor. The amino acid substitutions
responsible for these phenotypes were obtained by
selecting for intragenic, second-site mutations that restored
activity to a mutant repressor. These second-site
changes were then separated from the primary mutation,
and the DNA binding properties of repressors bearing
only the revertant changes were studied. |
| Comments |
lac repressor at 22°C, 200 mM KCl, reasonably physiological except perhaps for the 5% DMSO. Value arrived at by dividing Koff (0.022sec^-1, BNID 106393) by equilibrium dissociation constant (7.9×10^-10M, BNID 106391). See note beneath table |
| Entered by |
Uri M |
| ID |
106392 |