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- W99278894 abstract "ABSTRACT The structure and overall function of the T4 DNA replication complex has been outlined by Alberts a coworkers. In order to further refine this picture we have been studying the molecular details of the intera tions of some of the proteins of this replication syst with relevant nucleic acid lattices, and with one another. We have shown that gene 32-protein binds to short ( l = 28 residues) oligo nucleotides essentially independently of base composition or sugar type; this binding is also relatively independent of salt concentration. In contrast, the cooperative binding of gene 32-protein to poly nucleotides shows an appreciable dependence on base composition and sugar-type, and a large dependence on salt concentration. This salt concentration dependence resides in the binding constant to the nucleic acid lattice (K), and not in the coopera tivity parameter (ω); it has been shown that this salt concentration dependence involves a significant anion, as well as a cation, displacement reaction on binding. These results are interpreted in terms of an explicit two-conformation model of the interaction of this protein with nucleic acid lattices. In addition, the results provide a quantitative molecular interpretation of the autogenous regulation by this protein of its own synthesis, and lead to general principles for the development of binding specificity via cooperative (cluster) protein binding." @default.
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- W99278894 date "1980-01-01" @default.
- W99278894 modified "2023-09-26" @default.
- W99278894 title "MOLECULAR ASPECTS OF THE INTERACTIONS OF T4-CODED GENE 32-PROTEIN AND DNA POLYMERASE (GENE 43-PROTEIN) WITH NUCLEIC ACIDS" @default.
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- W99278894 doi "https://doi.org/10.1016/b978-0-12-048850-6.50047-8" @default.
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