Study Guide for Enzymes and Protein Purification Techniques

These flashcards cover key vocabulary and concepts related to enzymes and protein purification techniques.

Enzymes

Protein molecules that act as catalysts for biological reactions.

Catalysts

Substances that speed up the rate of a chemical reaction without being changed themselves.

Specificity

Enzymes are highly specific, performing one type of reaction with specific substrates.

Active Site

The region of the enzyme where the reaction occurs, typically a pocket that binds specific substrates.

Lock-and-Key Model

The active site of the enzyme is complementary in shape to the substrate.

Induced-Fit Model

The enzyme changes shape upon substrate binding, forming a snug fit around the substrate.

Cofactors

Non-protein substances required for enzyme function, can be inorganic ions or organic molecules.

Holoenzyme

An enzyme with its cofactor.

Apoenzyme

An enzyme without its cofactor.

Turnover Number

The maximum number of substrate molecules reacted upon by one molecule of enzyme in a certain amount of time.

Free Energy (ΔG)

A measure of energy capable of doing work; enzymes do not alter ΔG of a reaction.

Oxidoreductases

Enzymes that catalyze oxidation-reduction reactions.

Transferases

Enzymes that catalyze the transfer of groups from one molecule to another.

Hydrolases

Enzymes that catalyze the hydrolysis of substrates.

Vitamins

Essential organic molecules required in trace amounts, often precursors to coenzymes.

Antioxidants

Substances that prevent oxidation by becoming oxidized themselves.

Isoelectric Focusing

An electrophoresis method that separates proteins based on their isoelectric point.

SDS-PAGE

A technique used to separate proteins based on their molecular weight.

Affinity Chromatography

A purification technique that separates proteins based on their specific binding interactions.

Ion-Exchange Chromatography

A technique that separates proteins based on their charge.