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The C2 and C1 domains of some Protein Kinase C Enzymes are tethered through electrostatic and hydrophobic interactions in the inactive form. We have delineated the interaction surfaces of the C2 and C1A domains as shown in this figure. Upon PKC interacting with the cell membrane in a calcium and phosphatdiylserine specific manner, the C2-C1A tether is unleashed leading to C1A-diacylglycerol coordination and activation of the enzyme.

Contact Information

• Adjunct Assistant Professor of Chemistry & Biochemistry
  
• Office: 143 Raclin-Carmichael Hall
• Phone: 631.5054
• Contact by Email
• Group Website

Primary Research Areas

• Biochemistry

Research Specialties

• Drug Design & Discovery
• Molecular and Cell Biology
• Nanotechnology
• Structural Biology
• Theoretical & Computational Chemistry
• Biophysics
• Molecular Medicine

Lab Personnel

• Emmanuel AduGyamfi
• Christopher Gunasekaran
• Jordan Scott
• Katherine A. Ward
• Hui Yu
• Christina Cossell, M.S.
  Technician
• Lauren Buck
  Undergraduate
• David Cherney
  Undergraduate
• Yi Xue, M.D.
  Research Scientist
• Sophia Cortez
  ESTEEM M.S. student
• Deborah Olmstead
  Undergraduate
• Amanda Zofkie
  Undergraduate
• Katie Merriam
  Undergraduate
• 
  

Courses

• Special Topics in Biochemistry
• Membrane Biochemistry & Transport