Sonika Gill

 Sonika Gill
Mentor: Dr. Robert McKenna
College of Medicine
 
"I got involved research because I wanted to further explore my interest in Biochemistry. I plan to use this opportunity to gain experience in the research field in hopes of pursuing a career in biomedical research."

Major

Biology

Minor

Anthropology

Research Interests

  • Protein Structure
  • Protein Stability
  • Biochemistry

Academic Awards

  • UF University Scholars Program

Organizations

  • Indian Student Association
  • Heal the World
  • Gator Bhangra Club

Volunteer

  • Balance 180 Gymnasium
  • Center for Leadership and Service: Motiv8
  • Shands Volunteer Services

Hobbies and Interests

  • Dancing
  • Drawing
  • Movies
  • Volunteering

Research Description

Stability Enhancment of Human Carbonic Anhydrase II for Medical Applications
Human carbonic anhydrase II (HCAII) is a zinc-metalloenzyme that catalyzes the hydration of carbon dioxide to produce bicarbonate and a proton. This reaction has a turnover rate of 10^6 s-1, making it a highly efficient catalyst and one of the fastest enzymes known. HCAII has been of much interest in the development of medical devices such as artificial lungs. The current model of artificial lungs is encountering many problems in developing a smaller and more efficient device. In this model, the transfer of carbon dioxide is inefficient across the polymetric hollow fiber membranes (HFM), or the blood-gas interface, which causes the device to have a large surface area (1-2 m^2). The large surface area leads to issues with biocompatibility and hemocompatibility. Therefore, project I am proposing focuses on designing a more thermostable variant of HCAII that could increase its longevity within the artificial lung system. The presence of aromatic ring clusters is believed to impart thermostability to proteins. Using this information, I aim to design a more thermostable variant of HCAII by site-directed mutagenesis of the unique aromatic cluster residues found in HCAIV, one of the more stable HCAs known, into the respective sites in HCAII, without decreasing the catalytic efficiency of HCAII. To analyze these HCAII variants, I will be utilizing various biophysical methods including differential scanning calorimetry, isotope-labeled mass spectrometry, and X-ray crystallography to determine the melting temperature, kinetic activity, and structure, respectively. If these proposed mutations enhance the thermostability of HCAII, we will work in collaboration with another lab to design a more efficient artificial lung system.