title: The first 37 residues are sufficient for dimerization of ribosomal L7/L12 protein.
abstract: The ribosomal protein L7/L12 with the substitution of Cys38 for the Val38 residue was obtained and studied to test the orientation of polypeptide chains in the N-terminal region of the dimer. The results show that the L7/L12 dimer has a parallel (head-to-head) orientation of subunits and that its first 37 N-terminal residues are sufficient for dimerization.
authors.affiliation: Institute of Protein Research, Russian Academy of Sciences, Moscow Region.
authors.forename: A T
authors.initials: AT
authors.lastname: Gudkov
authors.forename: E V
authors.initials: EV
authors.lastname: Budovskaya
authors.forename: N M
authors.initials: NM
authors.lastname: Sherstobaeva
mesh_terms: D004926:Escherichia coli / Q000737:chemistry; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D014176:Protein Biosynthesis; D017433:Protein Structure, Secondary; D012269:Ribosomal Proteins / Q000737:chemistry*; D012270:Ribosomes / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D046911:Macromolecular Substances; D012269:Ribosomal Proteins; C016700:ribosomal protein L7-L12