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Green Fluorescent Protein. a B/MB senior seminar brought to you by Colm O’Carroll. This presentation will cover . The structural aspects of GFP which make fluorescence possible The advantages of using GFP and GFP mutants over other fluorescent markers

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green fluorescent protein

Green Fluorescent Protein

a B/MB senior seminar

brought to you by Colm O’Carroll

this presentation will cover
This presentation will cover
  • The structural aspects of GFP which make fluorescence possible
  • The advantages of using GFP and GFP mutants over other fluorescent markers
  • The use of GFP to monitor viral movement in plants
gfp s unique structure
GFP’s unique structure
  • Composed of 238 amino acids
  • “Paint in a can”
  • Each monomer composed of a central -helix surrounded by an eleven stranded cylinder of anti-parallel -sheets
  • Cylinder has a diameter of about 30A and is about 40A long
  • Fluorophore located on central helix
the fluoropore active site
The Fluoropore Active Site
  • Ser65-Tyr66-Gly67
  • Deprotonated phenolate of Tyr66 is cause of fluorescence
  • Forster Cycle (1949-Theodor Forster)
  • Proton transfer to His148
fluorophore formation
Fluorophore formation
  • One limitation of wtGFP is its slow rate of fluorescence acquisition in vivo
  • Renaturation most likely by a parallel pathway
  • Oxidation of Fluoropore (2-4 hours)
  • Two step process