GFP Structure and Function Questions

The video tutorial introduces Green Fluorescent Protein (GFP), originally isolated from the jellyfish Aequorea Victoria. GFP is a small protein composed of 238 amino acids and is a vital tool in molecular biology, earning scientists a Nobel Prize in 2008. The structure of GFP is a beta-barrel containing a chromophore responsible for its fluorescence. This chromophore absorbs blue or ultraviolet light, causing the phenoxy ring of tyrosine to become excited and emit bright green light. GFP is widely used in research as a reporter to indicate gene transcription and can be fused with other proteins to study their expression using fluorescence microscopy.

Where was GFP first isolated from?

• Moon jelly

• Pacific sea nettle

• Atlantic salmon

• Aequorea Victoria jellyfish

How many amino acids make up GFP?

• 238

• 150

• 300

• 200

What is the structural shape of GFP?

• Alpha helix

• Gamma loop

• Beta sheet

• Beta barrel

Which amino acids form the chromophore in GFP?

• Serine, Tyrosine, Glycine

• Alanine, Glycine, Serine

• Tyrosine, Phenylalanine, Glycine

• Serine, Alanine, Tyrosine

What type of light does the chromophore in GFP absorb?

• Blue or ultraviolet light

• Green light

• Red light

• Infrared light

What is the role of GFP in fluorescence microscopy?

• To absorb red light

• To absorb infrared light

• To emit blue light

• To emit green light

In research, what is GFP commonly used as?

• A catalyst

• A reporter

• An enzyme

• A substrate

What is a chimera in the context of GFP?

• A fusion of two different proteins

• A DNA sequence

• A type of jellyfish

• A fluorescent dye

Which promoter is active in the mechanosensory neurons of C. elegans?

• PMEC

• PMAC

• PMAK

• PMIC