Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9882194 | Archives of Biochemistry and Biophysics | 2005 | 12 Pages |
Abstract
The energetics of LRP binding to a 104 bp lac promoter determined from ITC measurements were compared to the energetics of binding to a shorter 40 bp DNA duplex with the 21 bp promoter binding site sequence. The promoter binding affinity of 2.47 ± 0.01 Ã 107 Mâ1 was higher than the DNA binding affinity of 1.81 ± 0.67 Ã 107 Mâ1 while the binding enthalpy of â804 ± 41 kJ molâ1 was lower than that of the DNA binding enthalpy of â145 ± 16 kJ molâ1 at 298.15 K. Both the promoter and DNA binding reactions were exothermic in phosphate buffer but endothermic in Tris buffer that showed the transfer of four protons to LRP in the former reaction but only two in the latter. A more complicated dependence of these parameters on temperature was observed for promoter binding. These energetic differences are attributable to additional LRP-promoter interactions from wrapping of the promoter around the LRP.
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Authors
Jayanthi Ramprakesh, Frederick P. Schwarz,