The form absorbs ultraviolet light (UV) at approximately 395

The primary
structure of GFP is a long polypeptide chain of 238 amino acids (Remington,
2011). When arranged into the tertiary structure, GFP forms an eleven stranded -barrel
with an -helix
inside (Remington, 2011). Three amino acids: tyrosine 66, serine 65, and
glycine 67 are centered within the -helix
(Remington, 2011). In the presence of oxygen, the amino acids get oxidized and
form a mature GFP chromophore (Remington, 2011). For the fluorescence of the
matured GFP chromophore, it must exist in one of two forms: the neutral
protonated/A form or the anionic/B form (Remington, 2011). The A form absorbs
ultraviolet light (UV) at approximately 395 nm whereas the B form absorbs light
in the blue range (approximately 475 nm) (Remington, 2011). As a fluorescent
tag, GFP has advanced studies in protein localization, gene expression, and
protein-protein interactions (Murayama
and Kobayashi 2014).

A protein of interest can be fused with a 714 base pair gfp at its N- or C- termini to visualize the target proteins
interactions in real time (Murayama
and Kobayashi
2014). Talk about other colors.

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