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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 l.jpg

Green Fluorescent Protein

a B/MB senior seminar

brought to you by Colm O’Carroll


This presentation will cover l.jpg
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 l.jpg
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 l.jpg
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 l.jpg
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


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