همایش ملی بیوانفورماتیک ایران

صفحه اصلی / 4th international edition and 13th Iranian Conference on Bioinformatics

Bioinformatics studies on S35K mutation on Mnemiopsin 2 photoprotein

نویسندگان :

ََAmirReza Mohammadi¹ Vahab Jafarian² Fatemeh Khatami³

1- University of Guilan 2- University of Guilan 3- University of Guilan

کلمات کلیدی :

Bioinformatics،Bioluminescence،Homology Modeling،Mnemiopsin 2

چکیده :

Bioluminescence is the process where certain living organisms emit light. This phenomenon occurs in photoproteins when Ca²⁺ binds to their EF-hand loops. Mnemiopsin 2 is a Ca²⁺-regulated photoprotein that contains three EF-hand motifs capable of binding Ca²⁺. The coelenterazine-bound form is called a photoprotein, while the protein without coelenterazine is referred to as an apophotoprotein. The S35K mutation is analyzed using professional bioinformatics servers and resources. A BLAST search in the NCBI database identifies S35K as an optimal choice due to direct evolution. Multiple 3D models of the S35K-mutated Mnemiopsin 2 photoprotein are modeled using Modeller v10.4, and these structures are evaluated with parameters such as ERRAT, Verify3D, and Ramachandran score, all accessible via the SAVES website. The Chimera software calculates the RMSD score, which allows the identification of the most accurate and reliable structural model. The selected model undergoes further assessment with the VADAR server. The Expasy server calculates the hydropathy index (based on the Kyte & Doolittle protocol), molecular weight, and instability index. The results show no significant differences in hydrogen bond distances or folding patterns, including alpha helices, beta sheets, and coil percentages, compared to the wild-type Mnemiopsin 2 photoprotein. A detailed comparison performed using Chimera indicates no observable structural changes between the mutated and wild-type photoproteins. This comprehensive analysis suggests that the S35K mutation is non-destructive, and the protein likely retains functionality similar to the wild type, with no significant reduction in stability. Additionally, this mutation decreases the hydropathy of the protein, making it an intriguing candidate for further functional studies and potential biotechnological applications.

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