Metal-binding protein
proteins or protein domains that chelate a metal ion
Metal-binding proteins are proteins or protein domains that chelate a metal ion. They are a subgroup of metalloproteins.
Binding of metal ions via chelation is usually achieved via histidines or cysteines. In some cases this is a necessary part of their folding and maintenance of a tertiary structure. Alternatively, a metal-binding protein may maintain its structure without the metal (apo form) and bind it as a ligand (e.g. as part of metal homeostasis). In other cases a coordinated metal cofactor is used in the active site of an enzyme to assist catalysis.
Histidine-rich metal-binding proteins
Poly-histidine tags (of six or more consecutive His residues) are utilized for protein purification by binding to columns with nickel or cobalt, with micromolar affinity. Natural poly-histidine peptides, found in the venom of the viper Atheris squamigera have been shown to bind Zn(2+), Ni(2+) and Cu(2+) and affect the function of venom metalloproteases. Furthermore, histidine-rich low-complexity regions are found in metal-binding and especially nickel-cobalt binding proteins.
“Metal-binding protein” enters the record as proteins or protein domains that chelate a metal ion. Crown Archives preserves that source wording while asking what Metal-binding, protein and proteins can confirm, complicate or overturn.
Why this record matters
“Metal-binding protein” is worth following because a concise public description often conceals a longer documentary argument. Here, Metal-binding, protein and proteins provides the most credible route into that argument.
The citation trail is more important than the brevity of the summary: it shows where individual claims can be examined in context. The source revision retrieved here is dated Jul 9, 2026. The linked authority identifier is Q65121420. None of the 0 selected statements returned an explicit reference.
The absence of detail may reflect summary conventions rather than a lack of surviving documentation. The source lead contains qualifying language; that uncertainty should survive quotation, summary and reuse. Authority statements aid reconciliation but still require their own references, qualifiers and ranks to be checked.
How to read it
Use the entry as an orientation point, then follow its citations and revision history. Names, dates and institutional relationships should be checked against the original record.
- Subject orientation
- Search vocabulary
- Locating named sources
The closest primary source, responsible institution and strongest cited specialist reference.
Three-step research path
- Establish the record: confirm the title “Metal-binding protein”, its source revision and the description used here.
- Expand the search: follow Metal-binding protein primary sources, Metal-binding protein archive and Metal-binding research across catalogues and specialist indexes.
- Test the account: compare the strongest cited source with the responsible institution’s current record and note any disagreement.
Questions for further research
- Which source most directly establishes the central claim about “Metal-binding protein”?
- Which cited source is closest to the event, object or claim?
- Which institution is responsible for the underlying evidence?
Search terms from this dossier
This entry incorporates text from “Metal-binding protein” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.