Proteins - The Molecular Workforce of the Oral Cavity

Vocabulary flashcards covering key proteins, structural interactions, and biochemistry concepts relevant to oral health based on Lecture 1.

Acquired Pellicle

An acellular, transparent film made from salivary proteins, glycoproteins, lipids, and carbohydrates that forms on tooth surfaces to help maintain mineral balance and shield enamel from minor erosive acids.

Collagen

A structural protein that maintains the integrity of gingiva, periodontal ligament, and dentin, requiring hydrogen bonds for stabilization.

Mucins

Salivary proteins in the lubrication and protection category that lubricate oral tissues and form protective coatings.

Histatins

Histidine-rich salivary proteins involved in innate defense that display antimicrobial activity against oral pathogens by using positive charges to interact with negatively charged microbial surfaces.

Secretory IgA

An adaptive immunity protein that prevents microbial adherence and supports mucosal immunity, stabilized by covalent disulfide bonds formed by cysteine residues.

Statherin

A salivary protein involved in mineral homeostasis that maintains calcium and phosphate balance and helps protect enamel.

Salivary Amylase

A digestive protein that initiates starch digestion in the oral cavity and relies on hydrophobic interactions for folding to form its three-dimensional active site.

Enzymes

Proteins that serve a catalysis function by accelerating biochemical reactions essential for life.

Hydrogen Bonds

Interactions whose primary role is to stabilize secondary and tertiary protein structure, such as within collagen.

Ionic Interactions

Charge-dependent interactions that stabilize charged regions and molecular interactions, such as promoting histatin binding to microbial surfaces.

Hydrophobic Interactions

The major driving force behind protein folding, occurring as nonpolar side chains cluster together to avoid contact with water in an aqueous environment.

Disulfide Bonds

Covalent interactions formed by cysteine residues that provide covalent stabilization to extracellular proteins.

Protein Denaturation

The process where environmental changes such as extreme pH, heat, organic solvents, or chemical denaturants disrupt stabilizing interactions, leading to a loss of protein structure and function.

Protein Misfolding

A state in which a protein is produced successfully but fails to fold correctly, resulting in reduced stability, loss of function, altered binding, or disease.