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Structure Prediction of the Bombyx mori Sericin 4 Protein

Khushnudbek EshchanovDepartment of Chemistry, Urgench State University, Urgench, UzbekistanDono BabadjanovaDepartment of Chemistry, Urgench State University, Urgench, UzbekistanMukhabbat BaltaevaDepartment of Chemistry, Urgench State University, Urgench, Uzbekistan

Proceedings of Pakistan Academy of Sciences A Physical and Computational Sciencesjournal2025

ABI

Annotatsiya

Natural silk (Bombyx mori) has been found to contain sericin 1, sericin 2, sericin 3, and sericin 4 proteins. The sequence of amino acid residues in them has also been well studied. However, there is little information on the molecular structure of sericin 4. We conducted studies on the prediction of the sericin 4 molecule's structure using the AlphaFold3 and YASARA computational servers. Molecular dynamics simulations were performed in aqueous solution to evaluate the stability and determine the most favourable conformation of the predicted sericin 4 structure. We mainly used the ProSA-web, Ramachandran Z and Molprobity score to evaluate the predicted structure of sericin 4, and the reliability of the predicted model was determined. The predicted molecular structure serves as a preliminary, yet robust, model of sericin 4.

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Mavzular

Silk-based biomaterials and applications Silkworms and Sericulture Research Neurobiology and Insect Physiology Research

Identifikatorlar

DOI: 10.53560/ppasa(62-4)693

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