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Chloroacetamide-Linked Nucleotides and DNA for Cross-Linking with Peptides and Proteins
A. Olszewska, R. Pohl, M. Brázdová, M. Fojta, M. Hocek,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články
- MeSH
- acetamidy chemie MeSH
- cystein chemie MeSH
- DNA chemie MeSH
- histidin chemie MeSH
- konformace nukleové kyseliny MeSH
- konformace proteinů MeSH
- molekulární modely MeSH
- nukleotidy chemie MeSH
- peptidy chemie MeSH
- proteiny chemie MeSH
- transport elektronů MeSH
- Publikační typ
- časopisecké články MeSH
Nucleotides, 2'-deoxyribonucleoside triphosphates (dNTPs), and DNA probes bearing reactive chloroacetamido group linked to nucleobase (cytosine or 7-deazadaenine) through a propargyl tether were prepared and tested in cross-linking with cysteine- or histidine-containing peptides and proteins. The chloroacetamide-modifed dNTPs proved to be good substrates for DNA polymerases in the enzymatic synthesis of modified DNA probes. Modified nucleotides and DNA reacted efficiently with cysteine and cysteine-containing peptides, whereas the reaction with histidine was sluggish and low yielding. The modified DNA efficiently cross-linked with p53 protein through alkylation of cysteine and showed potential for cross-linking with histidine (in C277H mutant of p53).
Citace poskytuje Crossref.org
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- $a Nucleotides, 2'-deoxyribonucleoside triphosphates (dNTPs), and DNA probes bearing reactive chloroacetamido group linked to nucleobase (cytosine or 7-deazadaenine) through a propargyl tether were prepared and tested in cross-linking with cysteine- or histidine-containing peptides and proteins. The chloroacetamide-modifed dNTPs proved to be good substrates for DNA polymerases in the enzymatic synthesis of modified DNA probes. Modified nucleotides and DNA reacted efficiently with cysteine and cysteine-containing peptides, whereas the reaction with histidine was sluggish and low yielding. The modified DNA efficiently cross-linked with p53 protein through alkylation of cysteine and showed potential for cross-linking with histidine (in C277H mutant of p53).
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