Protein Purification and Electrophoresis Methods

This set of flashcards covers key concepts related to protein purification and electrophoresis methods, focusing on techniques like SDS-PAGE, IEF, and 2-D PAGE.

Gel Electrophoresis

A versatile tool to separate, identify, and compare proteins based on charge, size, and abundance.

SDS-PAGE

A technique that uses sodium dodecyl sulfate to denature proteins and provide a uniform negative charge.

Isoelectric Point (pI)

The pH at which a protein has no net charge; key in IEF for protein separation.

2-Dimensional Gel Electrophoresis (2-D PAGE)

Combines isoelectric focusing and SDS-PAGE to separate proteins by both pI and molecular mass.

Polyacrylamide Gel

A matrix used in PAGE to separate proteins by charge and size.

Coomassie Brilliant Blue G-250

A dye that binds to basic amino acids, used to stain proteins in gels.

Molecular Mass Markers

Standards used to estimate the molecular mass of unknown proteins by comparing migration distances.

Buffer Chambers

Sections that hold the gel and provide ions for conductivity in the electrophoresis setup.

Pore Size

The size of spaces in the gel matrix; adjusted by acrylamide concentration to influence the resolution of proteins.

Migration Distance

The distance a protein moves through the gel, which is inversely proportional to its molecular mass in SDS-PAGE.