Laboratory Techniques in Biochemistry Quiz

Gel electrophoresis is a method that separates proteins based on their size by moving them through a gel matrix under an electric field.

SDS is a commonly used reagent in biochemistry to denature proteins by disrupting their structure and rendering them linear.

The Bradford assay is a method for quantifying protein concentration in a sample based on the dye binding capacity of proteins.

ELISA is used to detect and quantify the presence of specific antibodies or antigens in a sample.

Affinity chromatography separates biomolecules based on their specific interactions with a ligand, allowing for highly selective purification.

Gel electrophoresis is commonly used to separate DNA fragments based on their size by applying an electric field to a gel matrix.

Ion exchange chromatography separates proteins based on their net charge, allowing for purification by exploiting differences in charge.

Gas chromatography is not commonly used for protein quantification; other methods like Bradford assay or UV spectrophotometry are more suitable.

X-ray crystallography is a technique used to determine the three-dimensional structure of proteins by analyzing the diffraction pattern of X-rays from a crystalized protein sample.

Ethanol is not a common reducing agent in biochemistry; commonly used agents include DTT or β-mercaptoethanol.

A sonicator is used to disrupt cells and tissues, facilitating the release of cellular components for further analysis.

Tris-HCl is a commonly used buffer in protein electrophoresis, providing a stable pH environment for the separation of proteins.

Protease inhibitors are used to prevent enzymatic degradation of proteins during purification processes.