{
  "abstract": "Mini G proteins (miniG proteins) are engineered Gα constructs lacking the α-helical domain (AHD) and are widely used to stabilize active G protein-coupled receptor (GPCR) conformations for structural and biochemical studies. However, the intrinsic conformational and nucleotide-binding properties of miniG proteins remain incompletely understood relative to their full-length counterparts. Here, we compared miniGαi1 and full-length Gαi1 using fluorescence-based nucleotide-binding assays and hydrogen–deuterium exchange mass spectrometry (HDX-MS). BODIPY–FL–GTP assays showed that miniGαi1 interacted with GTP more rapidly and produced higher fluorescence intensity than full-length Gαi1. Unlike full-length Gαi1, miniGαi1 did not exhibit fluorescence decay following nucleotide binding, suggesting impaired or absent GTP hydrolysis activity. HDX-MS analysis demonstrated globally higher deuterium uptake in miniGαi1, particularly in regions associated with nucleotide binding and GPCR interaction. These results indicate that miniGαi1 adopts a more solvent-accessible and conformationally dynamic state than GDP-bound full-length Gαi1. Together, our findings provide biochemical and structural insight into the intrinsic properties of miniG proteins.",
  "abstract_shown": true,
  "affiliations": [
    "School of Pharmacy, Sungkyunkwan University, 2066 Seoburo, Jangan-gu, Suwon 16419, Republic of Korea"
  ],
  "article_type": null,
  "arxiv": null,
  "author_total": 2,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Longhan Duan"
    },
    {
      "affs": [
        0
      ],
      "name": "Ka Young Chung",
      "orcid": "0000-0001-9038-9571"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/537m302xwzgj4.bib",
  "cited_by": 0,
  "doi": "10.3390/ijms27219819",
  "fulltext_url": null,
  "id": "537m302xwzgj4",
  "issns": [
    "1422-0067"
  ],
  "landing_url": "https://www.mdpi.com/1422-0067/27/21/9819",
  "language": null,
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [],
  "openalex": null,
  "pdf_url": null,
  "pmcid": null,
  "pmid": null,
  "published": "2026-11-01",
  "publisher": "MDPI AG",
  "ris": "https://research.draconitic.com/paper/537m302xwzgj4.ris",
  "sources": [
    {
      "first_seen": "2026-11-05T00:20:58Z",
      "native_id": "10.3390/ijms27219819",
      "source": "crossref",
      "url": "https://www.mdpi.com/1422-0067/27/21/9819"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "issn:1422-0067",
      "subfield": "general"
    }
  ],
  "title": "Comparative Analysis of Conformational Dynamics and Nucleotide Binding in miniGαi1 and Full-Length Gαi1",
  "title_text": "Comparative Analysis of Conformational Dynamics and Nucleotide Binding in miniGαi1 and Full-Length Gαi1",
  "type": "peer-reviewed",
  "updated_at": "2026-11-06T00:21:14Z",
  "url": "https://research.draconitic.com/paper/537m302xwzgj4",
  "venue": "International Journal of Molecular Sciences",
  "versions": []
}