The majority of proteins contain a uniform positive charge, and a uniform neutral charge, and most proteins have intricate three-dimensional structures that might affect how well they travel through the gel electrophoresis. For these reasons, proteins need to be denatured. Here, the right answers are A, B, and D.
Protein separation is accomplished using a molecular technique called sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which operates in the proximity of an electric charge. Proteins are separated using SDS-PAGE according to their electrophoretic mobility. Protein charge, shape, and structure all affect electrophoretic mobility.
To proceed in the direction of the positive terminal, the protein molecules need to have a constant negative charge (anode). The overall charge of a protein is determined by the amino acid content of the protein as well as the charge of the individual amino acids.
Thus, depending on the total makeup of amino acids, the charge may change. Depending on the ratio of different amino acids, the total charge of the proteins can be positive, negative, or neutral. The SDS treatment gives the proteins a consistent, negative charge. Then, according to size, the negatively charged amino acids flow toward the positive terminal.
Complete question:
Proteins need to be denatured using an anionic detergent such as SDS before gel electrophoresis because: Select all that apply.
A - most proteins have a uniform positive charge
B - most proteins have complex three-dimensional structures that can impact their movement through the gel
C - the overall charge of a protein depends on the amino acid composition of the protein and can vary greatly
D - most proteins have a uniform neutral charge
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