Article

Structural preferences shape the entropic force of disordered protein ensembles

2023-01-21

Abstract excerpt

Intrinsically disordered protein regions (IDRs) make up over 30% of the human proteome and instead of a native, well-folded structure exist in a dynamic conformational ensemble. Tethering IDRs to a surface (for example, the surface of a well-folded region of the same protein) can reduce the number of accessible conformations in IDR ensembles. This reduces the ensemble’s conformational entropy, generating an effect...

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Literature Corpus work: 6c18f3c3-d7e8-547f-9a14-7bbe7933ca39
DOI: 10.1101/2023.01.20.524980

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