Bioinformatics Analysis of BMP15 Gene and Bone Morphological Protein-15 Sequence

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This study characterized the physicochemical properties and predicted the structure, function, and protein-protein interactions of bone morphogenetic protein 15 (BMP15) using bioinformatics tools. BMP15 was found to have a molecular weight of 45055.01 Daltons, sequence length of 392 amino acids, and an extinction coefficient of 55390 at 280 nm with a basic isoelectric point. Secondary structure analysis revealed BMP15 consists mostly of random coil (63.78%), followed by alpha helix (20.66%) and extended strand (15.56%) as well as beta turns. Amino acids with high coil structure like glycine and alanine, which are hydrophobic and flexible, represented the highest concentrations. Transmembrane helix prediction identified four helices located from inside to outside and three from outside to inside. SWISS-MODEL generated four protein structure models corresponding to sequences (Q6PX77.1. A, 5vqf.2. A, 5ntu.1. A, and 5hly.1. A) with sequence identities of (75.38%, 20.83%, 20.77% and 20.33%) respectively. Results correlate BMP15 with oocyte maturation and granulosa cell activation in follicular development. This comprehensive bioinformatics analysis of BMP15 properties, structure, and interactions provides a framework for further study of genetically inherited infertility, drug design, and new protein analysis.

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