Investigation of complexes formed between gene 32 protein from bacteriophage T4 and heavy-atom-modified single-stranded polynucleotides using optical detection of magnetic resonance
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00368a005
Reference52 articles.
1. T4 Bacteriophage Gene 32: A Structural Protein in the Replication and Recombination of DNA
2. Recent excitement in the DNA replication problem
3. Physicochemical properties of DNA binding proteins. Gene 32 protein of T4 and Escherichia coli unwinding protein
4. The methylmercury heavy atom effect. Phosphorescence polarization and triplet spin sublevel radiative activities of the methylmercury(II)-benzimidazole and methylmercury(II)-tryptophan complexes
5. Total Substitution of Bromodeoxyuridine for Thymidine in the DNA of a Bromodeoxyuridine-Dependent Cell Line
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1. Fluorescence, Phosphorescence, and Optically Detected Magnetic Resonance Studies of the Nucleic Acid Association of the Nucleocapsid Protein of the Murine Leukemia Virus,;Biochemistry;1997-05-01
2. Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA;Nature;1995-07
3. Protein: Nucleic acid interactions. I. Electronic structures of cytosine, indole, and guanine complexes;Biopolymers;1992-06
4. Physical studies of tyrosine and tryptophan residues in mammalian A1 heterogeneous nuclear ribonucleoprotein Support for a segmented structure;Journal of Molecular Biology;1991-09
5. Structure calculations for single-stranded DNA complexed with the single-stranded DNA binding protein GP32 of bacteriophage T4: a remarkable DNA structure;Biochemistry;1990-06-12
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