{
  "id": 13647032,
  "title": "Buried Ion-Pairs Reshape Folding Pathways of Artificial Proteins",
  "url": "https://urgent.news/2026/10/10/buried-ion-pairs-reshape-folding-pathways-of-artificial-proteins",
  "topic": "science",
  "section": "Science",
  "published": "2026-10-10T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.10.10.757878v1?rss=1"
  },
  "original_language": "en",
  "account": "Ion-pairs, charged motifs, play a crucial role in controlling the function of several proteins. However, the underlying physical principles behind the formation of ion-pairs during protein folding are not well understood. In this study, researchers demonstrate that buried ion-pairs in newly designed helical bundle proteins alter the folding pathways by introducing kinetic barriers. These barriers are eventually overcome through a hydrophobic collapse associated with the protein core's packing.\n\nThe researchers employed a combination of protein design, co-translational folding studies, nuclear magnetic resonance (NMR) spectroscopy, and molecular dynamics simulations to reach their findings. They discovered that introducing a buried ion-pair leads to a shifted folding transition, striking a balance between desolvation and electrostatic interactions within the protein and the surrounding solvent. Additionally, the folding pathway proves to be sensitive to changes in non-polar interactions and motifs that shield the ion-pair from its environment.\n\nThe authors' combined results offer a framework for comprehending how functional motifs influence protein folding and how alterations in charged networks impact protein stability.",
  "summary": "Ion-pairs are central charged motifs that control the biological function of several proteins. Yet, the physical principles linked to the formation of ion-pairs during protein folding remain poorly understood. Here, we show that buried ion-pairs of de novo-designed helical bundle proteins reshape the folding pathways by introducing kinetic barriers that are overcome by a hydrophobic collapse…",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 1,
    "also_reported_by": []
  },
  "ai_generated": true,
  "disclaimer": "Summaries, key points and the editor’s take are written by software from other outlets’ reporting and may contain errors — always check the linked original."
}