TY - JOUR
T1 - Energetics of cooperative binding of oligonucleotides with discrete dimerization domains to DNA by triple helix formation
AU - Distefano, Mark D.
AU - Dervan, Peter B.
PY - 1993/2/15
Y1 - 1993/2/15
N2 - Cooperativity in oligonucleotide-directed sequence-specific recognition of DNA by triple helix formation can be enhanced by the addition of discrete dimerization domains. The equilibrium association constants for cooperative binding of oligonucleotides that dimerize by Watson-Crick hydrogen bonds and occupy adjacent sites on double helical DNA by triple helix formation have been measured by quantitative affinity cleavage titration. For two oligonucleotides that bind unique neighboring 11-bp and 15-bp sites on double helical DNA, and dimerize by formation of an 8-bp Watson-Crick mini-helix, the free energy of binding is -8.0 and -9.7 kcal·mol-1, respectively, and the cooperative energy of interaction is -2.3 kcal·mol-1 (1 kcal = 4.18 kJ). The energetics of this artificial nucleic acid cooperative intermolecular assembly can mimic naturally occurring cooperative protein - DNA systems, such as the phage λ repressor.
AB - Cooperativity in oligonucleotide-directed sequence-specific recognition of DNA by triple helix formation can be enhanced by the addition of discrete dimerization domains. The equilibrium association constants for cooperative binding of oligonucleotides that dimerize by Watson-Crick hydrogen bonds and occupy adjacent sites on double helical DNA by triple helix formation have been measured by quantitative affinity cleavage titration. For two oligonucleotides that bind unique neighboring 11-bp and 15-bp sites on double helical DNA, and dimerize by formation of an 8-bp Watson-Crick mini-helix, the free energy of binding is -8.0 and -9.7 kcal·mol-1, respectively, and the cooperative energy of interaction is -2.3 kcal·mol-1 (1 kcal = 4.18 kJ). The energetics of this artificial nucleic acid cooperative intermolecular assembly can mimic naturally occurring cooperative protein - DNA systems, such as the phage λ repressor.
UR - http://www.scopus.com/inward/record.url?scp=0027536091&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027536091&partnerID=8YFLogxK
U2 - 10.1073/pnas.90.4.1179
DO - 10.1073/pnas.90.4.1179
M3 - Article
C2 - 8433980
AN - SCOPUS:0027536091
SN - 0027-8424
VL - 90
SP - 1179
EP - 1183
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 4
ER -