Circular dichroism studies on the zinc‐induced conformational changes in S‐100a and S‐100b proteins

FEBS Letters

Kay, Cyril M.¹  Mani, Rajam S.¹ 

[1] Medical Research Council Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

关键词: S-100 protein;    Ca2+ effect;    Zn2+ effect;    CD;    CD;    circular dichroism;    UV;    ultraviolet;    Tris;    tris(hydroxymethyl)aminoethane;    EDTA;    ethyl-enediaminetetraacetic acid;    DTT;    dithiothreitol;   

DOI  :  10.1016/0014-5793(83)80836-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effect of Zn²⁺ binding on the circular dichroism (CD) spectra of brain-specific S-100a and S-100b calcium-binding proteins has been examined. In the presence of Zn²⁺, S-100a undergoes a conformational change and the decrease in ellipticity at 222 nm, as a result of Zn²⁺ addition, was nearly 1400 deg.cm⁻².dmol⁻¹, whereas with S-100b there was no significant conformational change. Ca²⁺ was able to bind to S-100 proteins in the presence of Zn²⁺ and the two metal-ion binding sites on the proteins appear to be different. In the presence of Zn²⁺, K⁺ had not significant effect on the conformation of S-100 proteins. Ca²⁺ and Zn²⁺ binding induce different environments around the tyrosine residues in S-100a, whereas with S-100b, similar changes were observed for the single tyrosine residue, using either metal.

【 授权许可】

Unknown