Biochem 14.1 Protein Electrophoresis Concepts

A type of gel electrophoresis used to separate smaller molecules like proteins.

A type of gel electrophoresis used to separate larger molecules such as DNA and RNA.

A gel matrix that contains a large percentage of water and a relatively small percentage of a matrix-forming agent (agarose or polyacrylamide).

The percentage of the matrix-forming agent (agarose or polyacrylamide) in a gel, which influences the size of the pores.

The negatively charged electrode in an electrolytic cell, where reduction occurs.

The positively charged electrode in an electrolytic cell, where oxidation occurs.

The movement of charged particles through a gel matrix under the influence of an electric field.

The process of applying a negative charge to molecules, often done to prepare them for electrophoresis.

A type of electrophoresis used to separate molecules based on size and charge.

A mixture of molecules of known size and charge used in electrophoresis to estimate the sizes of the molecules in other lanes.

A staining molecule such as Coomassie that binds to proteins and colors them blue, allowing visualization of proteins in a gel.

A fluorescent dye such as ethidium bromide, often used in DNA and RNA gels, that binds to nucleic acids and fluoresces under UV light.

A type of visualization technique used to analyze DNA and RNA in gels, where the gel is exposed to UV light, causing the dye to fluoresce.

Native PAGE is a type of gel electrophoresis where proteins maintain their biological structure and function.

A mobility shift is a change in the migration rate of a protein during native PAGE due to its binding to another molecule, like a ligand.

A molecule that binds to a protein, often influencing its activity or function.

A complex formed when a ligand binds to a protein, influencing its behavior.

A type of gel electrophoresis that uses chemicals to denature proteins and separate them solely based on size.

Sodium dodecyl sulfate (SDS) is a strong detergent that breaks down protein structure. This is used in SDS-PAGE.

The process of removing the denaturing agent and allowing proteins to regain their original structure.

Disulfide bonds are chemical connections between cysteine amino acids in proteins. They can be broken with additional reagents.

The pH at which a molecule has no net electrical charge.

A measure of the molecule's net charge.

The size of a protein, often measured in kilodaltons (kDa).

The three-dimensional shape of a protein.

A protein's ability to move through the gel matrix.

The standard unit of measurement for DNA length, which is equal to one nucleotide pair.

A type of gel electrophoresis that does not break disulfide bonds.

A type of gel electrophoresis that breaks disulfide bonds, separating subunits.

A protein structure that contains multiple identical subunits linked by disulfide bonds.

Multiple identical subunits linked by disulfide bonds.

A protein structure that contains multiple distinct subunits linked by disulfide bonds.

Multiple distinct subunits linked by disulfide bonds.

A type of gel electrophoresis that separates proteins based on their isoelectric point (pI).

A technique that separates proteins based on their pI (isoelectric point). Proteins migrate through a pH gradient gel until they reach a pH equal to their pI, where they become neutral and stop migrating.

A technique that separates proteins based on their size. Proteins are denatured and given a negative charge, causing them to move towards the positive electrode (anode). Smaller proteins move faster through the gel.

Two-dimensional gel electrophoresis that combines IEF and SDS-PAGE. It separates proteins first by their pI and then by their size, providing a more detailed protein profile.

The process of denaturing proteins by breaking their structure. This allows for the separation of proteins based solely on size.

The process of restoring a protein's original structure after denaturation.

A mixture of molecules of known size and charge used as a reference in electrophoresis. It helps estimate the sizes of unknown molecules.

A stain that binds to proteins and makes them visible in a gel, allowing for visualization and analysis of protein bands.