Camel, Benjamin R.; Jose, Davis; Meze, Katarina; Dang, Anson; von Hippel, Peter H. published the artcile< Mapping DNA conformations and interactions within the binding cleft of bacteriophage T4 single-stranded DNA binding protein (gp32) at single nucleotide resolution>, Electric Literature of 452-06-2, the main research area is DNA binding domain bacteriophage T4 gp32 single nucleotide resolution.
In this study, we use single-stranded DNA (oligo-dT) lattices that have been position-specifically labeled with monomer or dimer 2-aminopurine (2-AP) probes to map the local interactions of the DNA bases with the nucleic acid binding cleft of gp32, the single-stranded binding (ssb) protein of bacteriophage T4. Three complementary spectroscopic approaches are used to characterize these local interactions of the probes with nearby nucleotide bases and amino acid residues at varying levels of effective protein binding cooperativity, as manipulated by changing lattice length. These include: (i) examining local quenching and enhancing effects on the fluorescence spectra of monomer 2-AP probes at each position within the cleft; (ii) using acrylamide as a dynamic-quenching additive to measure solvent access to monomer 2-AP probes at each ssDNA position; and (iii) employing CD spectra to characterize changes in exciton coupling within 2-AP dimer probes at specific ssDNA positions within the protein cleft. The results are interpreted in part by what we know about the topol. of the binding cleft from crystallog. studies of the DNA binding domain of gp32 and provide addnl. insights into how gp32 can manipulate the ssDNA chain at various steps of DNA replication and other processes of genome expression.
Nucleic Acids Research published new progress about Bacteriophage T4 protein Gp32 Role: BSU (Biological Study, Unclassified), BIOL (Biological Study). 452-06-2 belongs to class imidazoles-derivatives, and the molecular formula is C5H5N5, Electric Literature of 452-06-2.
Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem