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Titlebook: DNA-Ligand Interactions; From Drugs to Protei Wilhelm Guschlbauer (Director),Wolfram Saenger (Co Book 19871st edition The Editor(s) (if app

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https://doi.org/10.1007/978-3-030-72711-6llographic dyad. Each subunit is composed of six helices, five of which intertwine about each other in a way that may make it seemingly impossible to disengage the subunits without altering their tertiary structure. The two symmetrically related L-tryptophan binding sites are formed by this interfac
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Problem Description and Related Workes coding for the lactose enzymes. Genetic and biochemical data have implicated the N-terminal part or ‘headpiece’ of the repressor as the DNA binding domain.. The precise way in which . repressor recognizes its operator is, however, not known.
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Problem Description and Related Workis called DNA heteroduplex. A DNA heteroduplex is characterized by non-identical genetic information of the two complementary strands, such that upon DNA replication a single heteroduplex molecule segregates genetically, i.e. yields mixed progeny consisting of DNA duplexes with the sequence of indiv
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https://doi.org/10.1007/978-3-030-00238-1g sites. They cleave the DNA within or in the immediate vicinity of the recognition sequence. Because of the immense importance of these enzymes in analysis, preparation and in vitro recombination of DNA many investigations have been carried out to understand the structural and mechanistic features
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https://doi.org/10.1007/978-3-030-00238-1SIR method using a platinum isomorphous derivative [1,2,3]. Refinement is in progress. The endonuclease-DNA recognition complex consists of a distorted double helix and a protein dimer composed of identical subunits related by a two-fold axis of rotational symmetry (see Fig. 1). The distortions of t
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