Zinc finger proteins - Research Paper Example

folding characteristics but the most abundant and well studied is the classical “Cys2–His2” (Laity, Lee, and Wright 39) The nature of ZFP is such that they conveniently act as building blocks for many molecules and often occur in clusters. As such, their molecular nature permits them to be easily shuffled, duplicated or even altered through evolution. In the contemporary biotechnology world, they fit perfectly into re-engineering purposes and technology for numerous binding properties that find important use in research (Chang, Jiao, et al. 1426). ZFP and its high affinity for binding DNA is involved in binding of repressors and transcription activators which are very important in regulating expression of genes in a cell.

These ZPF have varied protein folds that dictate DNA binding of specific sequences like the helix-helix-turn which arouses the need to use them in therapy or research. ZFP have structural independence that are conserved and interconnected by linkers (Guo, Gaj and Barbas 96). These linkers are HC and named so because the first and last units are hystidine and cysteine residues. The hallmark radius and pitch of ZFP is gotten from H-C residues perfect interaction leading to right handed helix formation.

Zif268 which is a transcript factor contains triple finger domains where the α-helix interacts with the major groove of DNA (Mandel-Gutfreund, Baron and Margalit 141).Three consecutive DNA bases interact with all the three fingers through hydrogen bonds. Specificity of the interaction is derived from the interaction of the second positioned amino acid residue on the α-helix with the triplet of the secondary strand. In the end, the conserved residues undergo tertiary folding while each domain’s specificity is brought by the variable domains (Sumedha, Roy et al. 484). Control and regulation of gene expression has been shown to be an important aspect of ZFP through using specific selected three ZF peptides.

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