Module 3: Protein Analysis Review and Summary

These flashcards cover key vocabulary and concepts related to the analysis of proteins, including major techniques and important proteins discussed in Module 3.

Bradford Assay

A colorimetric assay for protein concentration, developed by Marion M. Bradford in 1976, where the absorbance at 595 nm is proportional to protein amount.

Peptide Bond

The bond formed between two amino acids in a protein by an amide linkage.

Absorbance (A)

The amount of light that a sample absorbs at a specific wavelength, used to measure concentration in spectrophotometry.

Beer-Lambert Law

A law stating that absorbance is directly proportional to concentration, expressed as A = εLc, where ε is the extinction coefficient, L is the path length, and c is the concentration.

SDS-PAGE

A technique used to separate proteins based on their molecular weight using polyacrylamide gel and sodium dodecyl sulfate.

Enzyme Activity

The rate at which an enzyme catalyzes a reaction, which can be measured to determine enzyme efficiency.

Lock-and-Key Model

A model describing how enzymes and substrates fit together precisely to catalyze a reaction.

Induced Fit Model

A model that describes how an enzyme changes shape to better fit the substrate upon binding.

Casein

A major protein in milk, constituting about 80% of the total milk protein, which is a phosphoprotein.

Whey Proteins

Proteins in milk that account for about 20% of the total milk protein, including substances like lactoferrin and immunoglobulins.

Colorimetric Methods

Techniques used to determine the concentration of substances based on color changes in reaction, such as the Bradford or Lowry assays.