title: Binding properties of T4 gene 32 protein fragments carrying partially cleaved terminal domains.
abstract: Analysis of fluorimetric equilibrium-binding isotherms of a proteolytic fragment of bacteriophage T4 gene 32 protein (g32P) lacking residues 1-9 shows that this region contains the site responsible for the function of the NH2-terminal 'B' domain (residues 1-21). The end codon of the frameshift mutant g32P-PR201 has been identified as TAG at nucleotide position 852. The PR201 gene 32 product ends at Ser283 and carries a truncated COOH-terminal 'A' domain (residues 253-301). Fluorimetric titrations of g32P-PR201 with double-stranded DNA show that the functional residues of the A domain are located within the region spanning residues 284-301.
authors: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06510.
authors: J R
authors: JR
authors: Casas-Finet
mesh_terms: D000596:Amino Acids / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D004279:DNA, Viral / Q000378:metabolism; D005453:Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013604:T-Phages / Q000235:genetics* / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D000596:Amino Acids; D004279:DNA, Viral; D014764:Viral Proteins