ChemInform Abstract: SAURE EIGENSCHAFTEN VON AQUOPLATIN(II)‐KOMPLEXEN

Grinberg, A.A.; Stetsenko, A. I.; Mitkinova, N. D.; Tikhonova, L. S.

doi:10.1002/chin.197115070

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“…Though the affinities of dCMP and dAMP are very close, the~ values for d(pC) 20 and d(pAho differ almost 50-fold. Basically the nucleotide sequence of the template determines its affinity to the enzyme, however the affinity of the above studied oligonucleotides to the enzyme was not stronger than that of d(pA) 20 (Kd -0.1 nM).…”

Section: Role Of Internucleotide Phosphate Groups Of the Template In mentioning

confidence: 87%

“…The Gibb 's energy of the complex made by the 3'-end of the primer and the enzyme is about -6.5 kcal/mol. At the same time, the contribution of complementary interactions of d(pT) 20 and d(pA) 10 is about -3.5 kcal/mol. The present model of the template and primer recognition by DNA polymerases helps to interpret some data obtained earlier.…”

Section: Role Of Internucleotide Phosphate Groups Of the Template In mentioning

confidence: 94%

“…Cis-(aquahydroxydiammine)platinum was prepared from cis-[Pt(NH 3 ) 2 Cl 2 ] according to (20). Mfinity reagents AR 1 and AR 2 wre prepared according to (10) with some modifications.…”

Section: Synthesis Of Pt 2 + -Modified Oligonucleotidesmentioning

confidence: 99%

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The Mechanism of Recognition of Templates By DNA Polymerases From Pro- and Eukaryotes as Revealed By Affinity Modification Data

Kolocheva

Nevinsky

Левина

et al. 1991

Journal of Biomolecular Structure and Dynamics

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Pt(2+)-containing derivatives of oligodeoxyribonucleotides were used to evaluate the ligand affinity to the template sites of Klenow fragment of DNA polymerase I from E. coli and DNA polymerase alpha from human placenta. The values of Kd and Gibb's energy (delta G degree) for the complexes of oligodeoxyribonucleotides and their derivatives with the template sites of these enzymes were determined from the effects protecting the enzyme from inactivation by Pt(2+)-containing oligonucleotides. Kd and delta G degree values of the complexes made by DNA polymerases and orthophosphate, triethylphosphate, d(pC)n, d(pT)n, d(pG)n, d(pA)n (where n = 1-25), heterooligonucleotides of various length and structure, and oligothymidylates with partially and completely ethylated internucleotide phosphates were evaluated. The obtained data enabled us to suggest 19-20 mononucleotide units of the template to interact with the protein. Only one template internucleotide phosphate forms a Me(2+)-dependent electrostatic contact (delta G = -1.1...-1.7 kcal/mol) and a hydrogen bond (delta G = -4.4...-4.9 kcal/mol) with the enzyme. It is likely that the mononucleoside units of the template form hydrophobic contacts with the enzymes. The efficiency of such interaction changes with the hydrophobicity of the bases: C less than T less than G approximately A. For both homo- and heterooligonucleotides the contributions of nucleoside units to the affinity of the templates to the enzymes is due to the complementary interactions with the primers. A hypothetical model for the template-primer interaction with DNA polymerases is suggested.

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Section: Role Of Internucleotide Phosphate Groups Of the Template In mentioning

confidence: 87%

Section: Role Of Internucleotide Phosphate Groups Of the Template In mentioning

confidence: 94%

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The Mechanism of Recognition of Templates By DNA Polymerases From Pro- and Eukaryotes as Revealed By Affinity Modification Data

Kolocheva

Nevinsky

Левина

et al. 1991

Journal of Biomolecular Structure and Dynamics

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ChemInform Abstract: SAURE EIGENSCHAFTEN VON AQUOPLATIN(II)‐KOMPLEXEN

Abstract: Durch potentiometrisch‐alkalimetrische Titration werden die jeweils 2 Konstanten der Säuredissoziation für die cis‐ und trans‐Isomeren der Aquokomplexe (Ia) sowie für die cis‐Isomeren der Komplexe (Ib) bestimmt.

Cited by 1 publication

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The Mechanism of Recognition of Templates By DNA Polymerases From Pro- and Eukaryotes as Revealed By Affinity Modification Data

The Mechanism of Recognition of Templates By DNA Polymerases From Pro- and Eukaryotes as Revealed By Affinity Modification Data

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