title: Femtomolar Zn(II) affinity of minimal zinc hook peptides--a promising small tag for protein engineering.
abstract: The minimal zinc hook peptide of Rad50 and its alanine mutants form highly stable Zn(II) complexes. These peptides were successfully used as a small, efficient tag for reversible Zn(II)-mediated protein homodimerization. The high stability, its biological consequences and potential applications in protein engineering are discussed.
authors.affiliation: Laboratory of Chemical Biology, University of Wrocław, ul. Tamka 2, 50-137 Wrocław, Poland.
authors.forename: Tomasz
authors.initials: T
authors.lastname: Kochańczyk
authors.forename: Piotr
authors.initials: P
authors.lastname: Jakimowicz
authors.forename: Artur
authors.initials: A
authors.lastname: Krężel
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D015202:Protein Engineering / Q000379:methods*; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D020027:Pyrococcus furiosus; D015032:Zinc / Q000378:metabolism*
chemical_list: D019843:Archaeal Proteins; D004268:DNA-Binding Proteins; D010446:Peptide Fragments; D015032:Zinc