Structure calculations for single-stranded DNA complexed with the single-stranded DNA binding protein GP32 of bacteriophage T4: a remarkable DNA structure
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00475a029
Reference33 articles.
1. The geometry of nucleic acids
2. The dimensions and shapes of the furanose rings in nucleic acids
3. Nucleic binding affinity of bacteriophage T4 gene 32 protein in the cooperative binding mode.
Cited by 12 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. C-terminal Domain of T4 gene 32 Protein Enables Rapid Filament Reorganization and Dissociation;Journal of Molecular Biology;2024-05
2. Dynamic structure of T4 gene 32 protein filaments facilitates rapid noncooperative protein dissociation;Nucleic Acids Research;2023-07-14
3. Mapping the interactions of the single-stranded DNA binding protein of bacteriophage T4 (gp32) with DNA lattices at single nucleotide resolution: gp32 monomer binding;Nucleic Acids Research;2015-08-14
4. Modulation of T4 gene 32 protein DNA binding activity by the recombination mediator protein UvsY;Journal of Molecular Biology;2008-07
5. Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA;Nature;1995-07
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