DNA Binding Properties of 2,7-Diazapyrene and ItsN-Methylated Cations Studied by Linear and Circular Dichroism Spectroscopy and Calorimetry

1997 ◽  
Vol 119 (25) ◽  
pp. 5798-5803 ◽  
Author(s):  
Hans-Christian Becker ◽  
Bengt Nordén
Keyword(s):  
Circular Dichroism ◽  
Dna Binding ◽  
Circular Dichroism Spectroscopy ◽  
Binding Properties ◽  
Dna Binding Properties ◽  
Circular Dichroïsm ◽  
And Calorimetry

Synthesis, crystal structure, DNA-binding and magnetism of copper 15-metallacrown-5 complexes based on glycinehydroxamic acid ligand

RSC Advances ◽  
2016 ◽  
Vol 6 (53) ◽  
pp. 47196-47202 ◽  
Author(s):  
Yanxia Meng ◽  
Hua Yang ◽  
Dacheng Li ◽  
Suyuan Zeng ◽  
Guifang Chen ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Circular Dichroism ◽  
Dna Binding ◽  
Fluorescence Spectroscopy ◽  
Calf Thymus Dna ◽  
Binding Properties ◽  
Acid Ligand ◽  
Calf Thymus ◽  
Dna Binding Properties ◽  
Circular Dichroïsm

Six lanthanide 15-MC-5 complexes based on glycinehydroxamic acid were synthesized. DNA-binding properties of the six complexes with calf thymus DNA were investigated using fluorescence spectroscopy and circular dichroism studies.

scholarly journals Conformational changes induced in Hoxb-8/Pbx-1 heterodimers in solution and upon interaction with specific DNA.

1997 ◽  
Vol 17 (9) ◽  
pp. 5369-5376 ◽  
Author(s):  
M Sánchez ◽  
P A Jennings ◽  
C Murre
Keyword(s):  
Circular Dichroism ◽  
Dna Binding ◽  
Conformational Changes ◽  
Gene Products ◽  
Homeodomain Proteins ◽  
Binding Properties ◽  
Hox Proteins ◽  
Structural Alterations ◽  
Dna Binding Properties ◽  
Circular Dichroïsm

Two classes of homeodomain proteins, Hox and Pbx gene products, have the ability to bind cooperatively to DNA. In Hox proteins, the homeodomain and a highly conserved hexapeptide are required for cooperative DNA binding. In Pbx, the homeodomain and a region immediately C terminal of the homeodomain are essential for cooperativity. Using fluorescence and circular dichroism spectroscopy, we demonstrated that Hox and Pbx proteins interact in the absence of DNA. The interaction in solution is accompanied by conformational changes. Furthermore, upon interaction with specific DNA, additional conformational changes are induced in the Pbx-1/Hoxb-8 heterodimer. These data indicate that prior to DNA binding, Hox-Pbx interaction in solution is accompanied by structural alterations. We propose that these conformational changes modulate the DNA binding properties of these proteins, ultimately resulting in cooperative DNA binding.

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