Biological Macromolecules and Protein

Protein

A molecule that performs many functions in the cell, including support, movement, transport, and metabolic regulation.

Amino Acid

The monomer that links together to form proteins; consists of a central carbon, hydrogen, carboxyl group, amino group, and a variable side chain (R group).

Polypeptide

A polymer of amino acids that forms when amino acids are linked together by peptide bonds.

Peptide Bond

The bond formed between the amino group of one amino acid and the carboxyl group of another during protein synthesis.

Enzyme

A type of protein that acts as a catalyst to increase the rate of metabolic reactions by lowering activation energy.

Activation Energy

The minimum energy that must be input to a chemical reaction in order for it to occur.

Substrate

The specific reactant on which an enzyme acts, fitting into the enzyme's active site like a key in a lock.

Specificity of Enzymes

The concept that each enzyme is specific to a particular substrate, facilitating only one type of reaction.

Hemoglobin

A protein responsible for transporting oxygen in the blood cells.

Functional Groups

The specific groups of atoms within molecules that are responsible for the characteristic reactions of those molecules; contribute to the diversity of amino acids.

Catalysis

The process by which an enzyme increases the rate of a reaction by lowering the activation energy.

Denaturation

The process in which proteins lose their natural structure due to external stress or compound, affecting their function.

Allosteric Regulation

The regulation of an enzyme's activity through the binding of an effector molecule at a site other than the active site.

Cofactor

A non-protein chemical compound that is required for the biological activity of a protein, often assisting enzymes.

Feedback Inhibition

A regulatory mechanism in which the accumulation of the end product of a metabolic pathway inhibits an earlier step in the pathway.

Isozyme

Different forms of an enzyme that catalyze the same reaction but are regulated differently.

Hydrophobic Interactions

Interactions that occur when nonpolar molecules aggregate to avoid contact with water, influencing protein folding.

Protein Folding

The physical process by which a protein takes on its complex, functional three-dimensional shape.