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The Bradford analysis is a procedure to measure the protein concentration in a solution. It is a subjective method. Hence, the results will depend on the composition of the amino acid. Marion M. Bradford developed the assay. He based it on the absorbency shift of the Coomassie Brilliant Blue G-250 dye. In acidic conditions, it goes from red to blue to bind the component. Two types of bond interaction take place during the formation of the complex. The Coomassie donates its free electron to the iron groups (Ibanez, 2007).
The second step of the Bradford analysis is the disruption of the protein's original state. Hence, it exposes its hydrophobic pockets, which are in the tertiary structure. They in turn have a non-covalent bond with the non-polar region of the dye. It happens through the van der Waals forces. They will position the positive amine groups near the negative charge of it. The ionic interaction become stronger than the initial one (Dennison, 2003).
The bond of the solution in Bradford analysis makes the blue form of the Coomassie dye stable. Therefore, the amount of this complex present is the measure of the protein concentration. The researcher can estimate it by using the absorbency reading. Historically, the absorption spectrum was at 595nm. There is also the cationic types, which are green or red.
Unlike other assays, the Bradford analysis is less susceptible to various chemical interference. There is the exception of Sodium dodecyl sulfate detergent.
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