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The T2M substitution in the gp100₂₀₉ tumor rejection antigen changes hydrogen bonds and cavities within the P2 pocket of HLA-A2. A hydrogen bond from the threonine to glutamate 63 of the protein is lost, as is a small cavity at the distal end of the P2 side chain. Thermodynamically, losing the hydrogen bond is expensive, but this is more than compensated for by filling the cavity. Thus, the T2M modification enhances peptide binding affinity, translating into improved immunogenicity.

See Borbulevych et al., Journal of Immunology 174, p. 4812 (2005).

Contact Information

• Associate Professor
  Director of Graduate Studies
• Office: 451 SHCB
• Phone: 574.631.9810
• Contact by Email
• Group Website

Primary Research Areas

• Biochemistry

Research Specialties

• Structural Biology
• Theoretical & Computational Chemistry
• Biophysics
• Molecular Medicine

Lab Personnel

• Brian E. Gloor
• Moushumi Hossain
• Francis K. Insaidoo
• Kurt H. Piepenbrink
• Daniel R. Scott
• Alison Wojnarowicz
  (Technician / Lab Manager)
• Oleg Borbulevych
  (Professional Specialist)
• Sujatha Santhanagopalan
  (Postdoctoral Fellow)
• Emily Doan
  (Technician)
• Priscilla Do
  (Undergraduate Researcher)

Courses

• Fundamentals of Biochemistry