A Model For The Mechanism Of Human Topoisomerase I Science The three dimensional structure of a 70 kilodalton amino terminally truncated form of human topoisomerase i in complex with a 22 base pair duplex oligonucleotide, determined to a resolution of 2.8 angstroms, reveals all of the structural elements of the enzyme that contact dna. the linker region that connects the central core of the enzyme to. The three dimensional structure of a 70 kilodalton amino terminally truncated form of human topoisomerase i in complex with a 22–base pair duplex oligonucleotide, deter mined to a resolution of 2.8 angstroms, reveals all of the structural elements of the enzyme that contact dna.
Dna Topoisomerase Function Structure Topoisomerase Inhibitors A model for the mechanism of human topoisomerase i. l. stewart, m. redinbo, 2 authors. j. champoux. published in science 6 march 1998. biology, chemistry. tldr. the three dimensional structure of a 70 kilodalton amino terminally truncated form of human topoisomerase i in complex with a 22 base pair duplex oligonucleotide reveals all of the. A model for the mechanism of human topoisomerase i. science 279, 1534–1541 (1998). article ads cas pubmed google scholar. Europe pmc is an archive of life sciences journal literature. the three dimensional structure of a 70 kilodalton amino terminally truncated form of human topoisomerase i in complex with a 22 base pair duplex oligonucleotide, determined to a resolution of 2.8 angstroms, reveals all of the structural elements of the enzyme that contact dna. The three dimensional structure of a 70 kilodalton amino terminally truncated form of human topoisomerase i in complex with a 22 base pair duplex oligonucleotide, determined to a resolution of 2.8 angstroms, reveals all of the structural elements of the enzyme that contact dna. the linker region that connects the central core of the enzyme to the carboxyl terminal domain assumes a coiled coil.
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