Protein would have to bind even tighter

Protein purification refers to processes whose intent is to
isolate either one or a few proteins from a mixture. The importance of this
process is that it is needed in order to properly characterize aspects of the
protein in interest – the protein’s function, its interactions with other
materials in the mixture, and its structure 1. Protein
purification can be used to separate proteins from non-proteins in a mixture or
to separate proteins from other proteins in a mixture. In this case, the
process used for protein purification was a resin column with the element
Nickel bound in the middle of the column to obtain only the proteins and remove
non-protein elements of the mixture. This would result in any substance without
histidine, which is an ?-amino acid that is used for protein biosynthesis 2, not binding to
the Nickel and flowing through the column. In order to remove the protein from
the column, it would require another step in protein purification that would
have to bind even tighter to the histidine than Nickel; this would be Imidazole,
our elution buffer. Imidazole has its ring structure incorporated into
histidine and is therefore able to compete with it for binding sites on Nickel,
allowing this solution to elute the protein from the column 3. In
this experiment, the sample loaded into the column was a green fluorescent
protein (GFP) without a linker 3.