Zinc fingers (ZFs) are among the most structurally diverse protein domains. They interact
with nucleic acids, other proteins and lipids to facilitate a multitude of biological processes …

Paramagnetic centers in biomolecules, such as specific metal ions that are bound to a
protein, affect the nuclei in their surrounding in various ways. One of these effects is the …

Pseudocontact shifts in biomolecular NMR using paramagnetic metal tags Page 1 1
Pseudocontact shifts in biomolecular NMR using paramagnetic metal tags Christoph …

A colorimetric assay has been developed for parallel detection of Cd2+, Ni2+ and Co2+
utilizing peptide-modified gold nanoparticles (P-AuNPs) as a sensing element based on its …

XPA is one of the key members of the protein complex of the nucleotide excision repair
(NER) pathway of DNA repair. The CCCC zinc finger domain of XPA is involved in the …

The Escherichia coli Zur protein is a Fur homologue that regulates expression of Zn (II)
uptake systems. The zinc-loaded form of Zur is proposed to bind DNA and repress …

Zinc finger transcription factors represent the largest single class of metalloproteins in the
human genome. Binding of Zn (II) to their canonical Cys4, Cys3His1, or Cys2His2 sites …

Xeroderma pigmentosum group A complementing protein (XPA) is a member of the protein
complex of the nucleotide excision repair (NER) pathway of DNA repair, participating in the …

Zinc is one of the most widespread metal ions found in biological systems. Of the expected
3000 zinc proteins in the human proteome, most contain zinc in structural sites. Among …

Zinc finger proteins utilize zinc for structural purposes: zinc binds to a combination of
cysteine and histidine ligands in a tetrahedral coordination geometry facilitating protein …