Construct · 1 fields · 1 citations

chaperone: a standalone construct

One name. One construct. A landmark on the map.

● anchor · a standalone construct Nearest construct by meaning·not indexed
chaperone1 CONSTRUCTMolecular chaperoneLASKEY ET AL. · 1978

A single standalone construct; nearby constructs are located against it in the Collider. Tap a field for its definition, unit, and measures.

Molecular biology

A protein that helps others fold without joining them

In molecular biology, a chaperone is a protein that helps other proteins or assemblies reach their correct folded or assembled state by binding them transiently and preventing wrong interactions, without being part of the finished structure itself. Laskey and colleagues' 1978 Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA first used the term for nucleoplasmin, which escorts histones onto DNA, and the idea was later generalised to the chaperones that assist folding under stress. The referent is an escort molecule defined by what it facilitates and then releases, measured by its effect on folding or assembly yield, and it shares only a metaphor with a human social chaperone.[1]

Unit
The improvement in correct folding or assembly attributable to the escort protein
Recovery means
Not applicable
Measured by
Assessed by folding or assembly yield and aggregation prevention in the chaperone's presence versus absence, and by its transient binding

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Nearby constructs

assembly1 fields · 1 citationsanchor · a standalone constructbeing3 fields · 3 citationsjingle · one word, three constructsbinding4 fields · 4 citationsjingle · one word, four constructs

References

  1. Laskey, R. A., Honda, B. M., Mills, A. D., & Finch, J. T. (1978). Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA. Nature, 275(5679), 416–420. https://doi.org/10.1038/275416a0

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