Objective: To analyze the structure and function of PYGO1 protein with bioinformatics.
Methods: The bioinformatic methods and tools were used to analyze the physical and chemical properties, transmembrane region, hydrophobicity and hyrdrophilicity, secondary structure and functional category of PYGO1 protein.
Results: The bioinformatic analysis revealed that proline content was the highest of all amino acid residues in PYGO1 protein; the molecular formula was C(1943)H(2937)N(577)O(635)S(18) with a relative molecular mass of 45; and the theoretical isoelectric point was 6.38. The analysis also demonstrated that PYGO1 was a hydrophilic and non-transmembrane protein; its main component was alpha-helix and random coil; it contained a plant homeodomain.
Conclusion: Human pygo1 gene may act as a transcription regulation factor to regulate the heart development and the progress of heart diseases.
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http://dx.doi.org/10.3785/j.issn.1008-9292.2014.06.002 | DOI Listing |
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