Back to search

Article

Assessing the helical stability of polyXYs at the boundaries of Intrinsically Disordered Regions with MD simulations

2024-11-18

Abstract excerpt

Intrinsically disordered regions (IDRs) in proteins lack stable structure. By carrying many hydrophilic and charged residues, it prevents them from forming globular domains and contributes to their flexibility and accessibility. Naturally, regions with reduced amino acid composition (low complexity regions; LCRs) occur within IDRs. Disorder and low complexity in protein sequences are linked to various biological f...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
d36060ee-c5e3-5d44-a1a1-33a72f5ec6f6
DOI
10.1101/2024.11.16.623902
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
Assessing the helical stability of polyXYs at the boundaries of Intrinsically Disordered Regions with MD simulationsDOI 10.1101/2024.11.16.623902
Select a neighboring publication to make it the new centre.