Bavoso A, Ostuni A, Battistuzzi G, Menabue L, Saladini M, Sola M
Department of Chemistry, University of Basilicata, Potenza, Italy.
Biochem Biophys Res Commun. 1998 Jan 14;242(2):385-9. doi: 10.1006/bbrc.1997.7974.
The metal binding properties of a 18-residue zinc finger peptide containing a CCHC box which reproduces one of the cysteine-rich domains of a putative nucleic acid binding protein encoded by the Fw transposable element from Drosophila melanogaster were investigated through electronic and 1H NMR spectroscopy. Dissociation constants of 2(+/- 1) x 10(-12) M and 4(+/- 1) x 10(-7) M were determined for the Zn2+ and Co2+ adduct, respectively. These values are similar to those for other CCHC-peptides investigated previously, although the length of the spacer between the second cysteine and the histidine apparently exerts some influence on the spectral properties and on the stability of the Co(2+)-peptide adduct. The 1H NMR spectrum of the present Co(2+)-derivative contains a number of well resolved hyperfine-shifted resonances between 350 and -50 ppm which arise from the metal binding residues and nearby groups. These peaks can in principle be profitably exploited to monitor protein-nucleic acid interactions.
通过电子光谱和1H核磁共振光谱研究了一种含有CCHC盒的18个残基的锌指肽的金属结合特性，该锌指肽复制了果蝇Fw转座元件编码的一种假定核酸结合蛋白的富含半胱氨酸结构域之一。分别测定了Zn2+和Co2+加合物的解离常数为2(±1)×10(-12)M和4(±1)×10(-7)M。这些值与之前研究的其他CCHC肽的值相似，尽管第二个半胱氨酸和组氨酸之间的间隔长度显然对光谱特性和Co(2+)-肽加合物的稳定性有一定影响。目前Co(2+)-衍生物的1H核磁共振谱在350至-50 ppm之间包含许多分辨率良好的超精细位移共振峰，这些峰来自金属结合残基和附近基团。原则上，这些峰可用于监测蛋白质-核酸相互作用。
