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Protein domain

conserved part of a protein

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General referenceInterpretive dossier study · Crown Archives visual atlas
Record originEnglish Wikipedia
Text licenseCC BY-SA 4.0
Source revisionSep 22, 2026
Entity authorityQ898273
Source-derived summary

In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and folds independently from the rest. Each domain forms a compact, folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. Domains vary in length from about 50 to 250 amino acids.

The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins.

Background

The concept of the domain was first proposed in 1973 by Wetlaufer after X-ray

crystallographic studies of hen lysozyme and papain and by limited proteolysis studies of immunoglobulins. Wetlaufer defined domains as stable units of protein structure that could fold autonomously.

Editorial summary

“Protein domain” enters the record as conserved part of a protein. Crown Archives preserves that source wording while asking what Protein, domain and conserved can confirm, complicate or overturn.

Editorial reviewA practical starting point whose main value is the path it opens into stronger specialist and primary sources. The current lead gives the account dated anchors—1973—that can be checked directly. The selected authority fields contribute no independent date. Its strongest next move is a source search built around Protein, domain and conserved.
Editorial analysis

Why this record matters

“Protein domain” is worth following because a concise public description often conceals a longer documentary argument. Here, Protein, domain and conserved provides the most credible route into that argument.

Evidence profile

Vocabulary and entity names are the principal evidence signals here, because they determine the precision of every later search. The source revision retrieved here is dated Sep 22, 2026. The linked authority identifier is Q898273. None of the 0 selected statements returned an explicit reference. The first chronological checks are 1973.

Critical limits

Overview language is designed for orientation and should not be treated as a substitute for the evidence cited beneath it. 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.

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The closest primary source, responsible institution and strongest cited specialist reference.

Three-step research path

  1. Establish the record: confirm the title “Protein domain”, its source revision and the description used here.
  2. Expand the search: follow Protein domain primary sources, Protein domain archive and Protein research across catalogues and specialist indexes.
  3. Test the account: compare the strongest cited source with the responsible institution’s current record and note any disagreement.

Questions for further research

  1. Which source most directly establishes the central claim about “Protein domain”?
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Source & attribution

This entry incorporates text from Protein domain” 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.