As a dedicated faculty member at the University of Baghdad, College of Sciences, Department of Biology, my major specialization is biology, and my minor specialization is molecular biology and genetic engineering. I am committed to advancing scientific knowledge through research, fostering student learning, and contributing to the academic community in these rapidly evolving fields.
As a highly motivated molecular biologist with a strong foundation in protein engineering, I excel at designing and optimizing biological systems to enhance their function. My expertise spans a range of advanced molecular techniques, including gene editing, recombinant DNA technology, rational protein engineering, non-canonical amino acid incorporation, selenomethionine incorporation into protein, high-throughput protein expression and purification, X-Ray crystallography, preparation of protein crystals, Click chemistry, PCR, oligonucleotide primers design, gel electrophoresis, DNA extraction, SDS-PAGE, DNA amplification, DNA purification, DNA quantification, recombinant protein expression, protein extraction, protein quantification, restriction digestion, bacterial transformation, preparation of competent cells, construction of expression vectors, plasmid cloning, plasmid extraction, ligation, cell lysis, and plasmid DNA isolation, as well as, AB binary toxins. I'm adept at leveraging bioinformatics tools for sequence analysis, solving three-dimensional structures experimentally, and protein modeling.
Protein engineering
Molecular biosciences
Molecular Biology and Genetic Engineering
Here we determined the structure of a cold active family IV esterase (EstN7) cloned
The Hbl toxin is a three-component haemolytic complex produced by Bacillus cereus sensu lato strains and implicated as a cause of diarrhoea in B. cereus food poisoning. While the structure of the HblB component of this toxin is known, the structures of the other components are unresolved. Here, we describe the expression of the recombinant HblL1 component and the elucidation of its structure to 1.36 Å. Like HblB, it is a member of the alpha-helical pore-forming toxin family. In comparison to other members of this group, it has an extended hydrophobic beta tongue region that may be involved in pore formation. Molecular docking was used to predict possible interactions between HblL1 and HblB, and suggests a head to tail dimer might f
... Show MoreFluorescent proteins (FPs) have revolutionised the life sciences, but the chromophore maturation mechanism is still not fully understood. Here we photochemically trap maturation at a crucial stage and structurally characterise the intermediate.
Construction of artificial higher order protein complexes allows sampling of structural architectures and functional features not accessible by classical monomeric proteins. Here, we combine in silico modelling with expanded genetic code facilitated strain promoted azide-alkyne cycloaddition to construct artificial complexes that are structurally integrated protein dimers and demonstrate functional synergy. Using fluorescent proteins sfGFP and Venus as models, homodimers and heterodimers are constructed that switched ON once assembled and display enhanced spectral properties. Symmetrical crosslinks are found to be important for functional enhancement. The determined molecular structure of one artific
Bacteria strain H7, which produces flocculating substances, was isolated from the soil of corn field at the College of Agriculture in Abu-Ghrib/Iraq, and identified as Bacillus subtilis by its biochemical /physiological characteristics. The biochemical analysis of the partially purified bioflocculant revealed that it was a proteoglycan composed of 93.2 % carbohydrate and 6.1 % protein. The effects of bioflocculant dosage, temperature, pH, and different salts on the flocculation activity were evaluated. The maximum flocculation activity was observed at an optimum bioflocculant dosage of 0.2 mL /10 mL (49.6%). The bioflocculant had strong thermal stability within the range of 30-80 °C, and the flocculating activity was over 50 %. The biofloc
... Show MoreUropathogenic specific protein is a genotoxic protein targeting the DNA, leading to mutations and modifications in the normal cell's DNA and subsequently, cancer development. This study aims to determine the prevalence of the usp gene in Uropathogenic Escherichia coli isolated from females with urinary tract infections and study its correlation with biofilm formation. One hundred and five urine specimens were collected from female patients (20 to 55 years old) with urinary tract infections attending hospitals. Traditional laboratory methods using selective and differential culture media were used for initial bacterial isolation and identification, and molecular techniques that targeted a segment of the 16SrRNA gene with a specific primer pa
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