Solid-phase synthesis, metal binding and folding properties of caulimovirus-related 'zinc finger'.
A 17-residue peptide containing the caulimovirus-related "zinc finger' was prepared by solid-phase peptide synthesis. Fluorescence measurements showed that the tryptophan quantum yield was Zn(2+)-dependent, allowing a 1:1 a stoichiometry for the complex to be determined. The structure of the peptide was characterized using circular dichroic spectroscopy, which indicates that the peptide exhibits a random coiled conformation in the absence of zinc but appears to form an ordered structure in the presence of zinc.
Ji
H
H
Department of Chemistry, Peking University, Beijing, China.
Zhang
R
R
Lai
L
L
Shao
M
M
D000595:Amino Acid Sequence; D017796:Caulimovirus / Q000737:chemistry*; D002942:Circular Dichroism; D008969:Molecular Sequence Data; D019251:Nucleocapsid / Q000737:chemistry* / Q000378:metabolism; D019590:Nucleocapsid Proteins; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D015032:Zinc / Q000378:metabolism; D016335:Zinc Fingers
D019590:Nucleocapsid Proteins; D010446:Peptide Fragments; C104528:nucleocapsid protein, Caulimovirus; D015032:Zinc