BIBC 100 Study Guide - Final Guide: Coelenterazine, Bioluminescence, Aequorin
Document Summary
Describe the structure and function of aequorin and gfp. Describe the structure of the gfp and mrfp chromophores. Explain how site-directed mutations result in gfp and mrfp derivatives of different colors. Describe how fluorescent proteins can be modified to detect molecules (calcium/metal ions) Explain how fret works and how it is used to examine protein interactions, protein activity or changes in calcium levels. Proteins in jellyfish aequorea victoria: aequorin: luminescent protein; after calcium binds, it emits photons of blue light, gfp: fluorescent protein; absorbs blue light photons to be excited, then emits green light photons. Aequorin: apoaequorin: aequorin without coelenterazine, coelenterazine: a prosthetic group that acts as a chromophore. Molecular oxygen required to generate peroxide form of coelenterazine. Energy from calcium- induced rearrangement triggers oxidative decarboxylation. This causes the nitrogen ring to open from loss of co2 and production of excited coelenteramide.
