Biochemical Characterization of Dystrophin Spectrin Type Repeats
Biochemical and Biophysical analysis of Dystrophin Spectrin Type Repeats with emphasis on structure prediction.
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The dystrophin gene and its association with dystrophies is a prime factor to study the spectrin type repeats (STR) of dystrophin. There are 24 triple helical rods of Dystrophin STRs having four flexible hinges. The exon skipping and tissue specifity of the dystrophin isoforms make its function diverse. The deletion of STRs and mutations causes instability of the protein leading to diseases. This work studies the stability of spectrin type repeat, which would identify the roles and probably understand the function of individual spectrin repeat in diseases. The repeats are subjected to urea and...
The dystrophin gene and its association with dystrophies is a prime factor to study the spectrin type repeats (STR) of dystrophin. There are 24 triple helical rods of Dystrophin STRs having four flexible hinges. The exon skipping and tissue specifity of the dystrophin isoforms make its function diverse. The deletion of STRs and mutations causes instability of the protein leading to diseases. This work studies the stability of spectrin type repeat, which would identify the roles and probably understand the function of individual spectrin repeat in diseases. The repeats are subjected to urea and temperature and the helical stability is measured. Structure prediction methods were worked on d1617 dystrophin spectrin double repeat to predict its structure which resulted in 4 angstrom resolution. The crystal structure could not be solved with low resolution but deduced the crystal conditions of face centered orthorhombic F222 space group for d1617. The STR stability and structure is important in medicine and gene therapy, which would aid in complementing against absent repeats or frame shift mutation in dystrophies and also aid in drug development.
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