@article{open3217,
          volume = {288},
          number = {138614},
           month = {February},
          author = {Madhumita Dey and Arpit Gupta and Maulik D Badmalia and  Ashish and Deepak Sharma},
           title = {Visualizing gaussian-chain like structural models of human {\ensuremath{\alpha}}-synuclein in monomeric pre-fibrillar state: Solution SAXS data and modeling analysis},
       publisher = {Elsevier BV},
            year = {2025},
         journal = {Int. J. Biol. Macromol.},
           pages = {138614},
        keywords = {ALPHAFOLD2; EOM; Monomer; Normal mode analysis; Protein structure; SAXS; {\ensuremath{\alpha}}-Synuclein},
             url = {http://crdd.osdd.net/open/3217/},
        abstract = {Here, using small angle X-ray scattering (SAXS) data profile as reference, we attempted to visualize conformational ensemble accessible prefibrillar monomeric state of {\ensuremath{\alpha}}-synuclein in solution. In agreement with previous reports, our analysis also confirmed that {\ensuremath{\alpha}}-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 C{\ensuremath{\alpha}} 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 {\ensuremath{\alpha}}-helical content best-represents non-associating monomeric {\ensuremath{\alpha}}-synuclein.}
}