{
      "number": 138614,
      "eprintid": 3217,
      "date": "2025-02",
      "userid": 2,
      "rev_number": 3,
      "creators": [
        {
          "name": {
            "lineage": null,
            "given": "Madhumita",
            "honourific": null,
            "family": "Dey"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Arpit",
            "honourific": null,
            "family": "Gupta"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Maulik D",
            "honourific": null,
            "family": "Badmalia"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": null,
            "honourific": null,
            "family": "Ashish"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Deepak",
            "honourific": null,
            "family": "Sharma"
          }
        }
      ],
      "dir": "disk0\/00\/00\/32\/17",
      "keywords": "ALPHAFOLD2; EOM; Monomer; Normal mode analysis; Protein structure; SAXS; α-Synuclein",
      "lastmod": "2026-02-02 07:16:35",
      "pagerange": 138614,
      "publisher": "Elsevier BV",
      "metadata_visibility": "show",
      "eprint_status": "archive",
      "status_changed": "2026-02-02 07:16:35",
      "volume": 288,
      "datestamp": "2026-02-02 07:16:35",
      "uri": "http:\/\/crdd.osdd.net\/open\/id\/eprint\/3217",
      "type": "article",
      "title": "Visualizing gaussian-chain like structural models of human α-synuclein in monomeric pre-fibrillar state: Solution SAXS data and modeling analysis",
      "abstract": "Here, using small angle X-ray scattering (SAXS) data profile as reference, we attempted to visualize conformational ensemble accessible prefibrillar monomeric state of α-synuclein in solution. In agreement with previous reports, our analysis also confirmed that α-synuclein molecules adopted disordered shape profile under non-associating conditions. Chain-ensemble modeling protocol with dummy residues provided two weighted averaged clusters of semi-extended shapes. Further, Ensemble Optimization Method (EOM) computed mole fractions of semi-extended ``twisted'' conformations which might co-exist in solution. Since these were only Cα traces of the models, ALPHAFOLD2 server was used to search for all-atom models. Comparison with experimental data showed all predicted models disagreed equally, as individuals. Finally, we employed molecular dynamics simulations and normal mode analysis-based search coupled with SAXS data to seek better agreeing models. Overall, our analysis concludes that a shifting equilibrium of curved models with low α-helical content best-represents non-associating monomeric α-synuclein.",
      "publication": "Int. J. Biol. Macromol."
    }