Protein Structure & Function Flashcards

Flashcards about protein structure and function.

Protein Functions

Proteins with diverse functions including enzymes, structural proteins, motor proteins, transporter proteins, storage, signaling proteins, receptors, and gene regulatory proteins.

Amino Acid Structure

Central carbon atom bonded to an amino group (H2N), a carboxyl group (COOH), a hydrogen atom (H), and a side chain (R-group).

Classes of Amino Acids

Nonpolar, polar, and electrically charged, based on the chemical composition of the R groups.

Non-Polar Amino Acids

R-groups are hydrocarbons; interaction with water is hydrophobic; bonding through hydrophobic interactions.

Polar Amino Acids

R-groups contain polar groups (carbonyls, hydroxyls, amines); interaction with water is hydrophilic; bonding through hydrogen bonding.

Polar Charged Amino Acids

R-groups are polar and carry a full charge; interaction with water is hydrophilic; bonding through ionic bonding.

Primary Protein Structure

Amino acid sequence, covalent bonds between amino acids.

Secondary Protein Structure

Alpha helix and beta pleated sheets, hydrogen bonding of the backbone.

Tertiary Protein Structure

Overall 3D shape of a single polypeptide, R-group interactions, all bond types.

Quaternary Protein Structure

Protein made up of multiple polypeptide chains/subunits, all bond types.

Protein Structure

Overall 3-dimensional structure of a protein is determined by the interactions of R-groups, including Van der Waals forces.

Protein Conformation

Final folded protein structure.

Chaperone Proteins

Specialized proteins that facilitate correct protein folding without dictating it; they increase the efficiency of proper folding by binding to hydrophobic regions.

Protein Structures

Form rings, filaments, sheets, and spheres; structure determines function.

Amyloid Structures

Stacks of beta-sheets in long rows that form when proteins misfold, damaging cells and tissues.

Prions

Misfolded proteins that convert properly folded proteins to a misfolded conformation, spreading through contaminated sources.

Protein Domain

Region of a protein that attaches to a substrate or another protein.

Disulfide Bonds

Covalent bonds between cysteine side chains that stabilize extracellular proteins.

Ligands

Molecules that bind specifically to proteins.

Enzymes

Bind specific substrates in the active site and speed up chemical reactions by lowering activation energy.

Protein Helpers

Small molecules that aid proteins, such as heme groups in hemoglobin and coenzymes (vitamins).

Protein Kinases

Enzymes that phosphorylate other proteins by attaching a phosphate group to an amino acid side chain, affecting protein shape and ligand binding.

Protein Functions

Proteins with diverse functions including enzymes, structural proteins, motor proteins, transporter proteins, storage, signaling proteins, receptors, and gene regulatory proteins.

Amino Acid Structure

Central carbon atom bonded to an amino group (H2N), a carboxyl group (COOH), a hydrogen atom (H), and a side chain (R-group).

Classes of Amino Acids

Nonpolar, polar, and electrically charged, based on the chemical composition of the R groups.

Non-Polar Amino Acids

R-groups are hydrocarbons; interaction with water is hydrophobic; bonding through hydrophobic interactions.

Polar Amino Acids

R-groups contain polar groups (carbonyls, hydroxyls, amines); interaction with water is hydrophilic; bonding through hydrogen bonding.

Polar Charged Amino Acids

R-groups are polar and carry a full charge; interaction with water is hydrophilic; bonding through ionic bonding.

Primary Protein Structure

Amino acid sequence, covalent bonds between amino acids.

Secondary Protein Structure

Alpha helix and beta pleated sheets, hydrogen bonding of the backbone.

Tertiary Protein Structure

Overall 3D shape of a single polypeptide, R-group interactions, all bond types.

Quaternary Protein Structure

Protein made up of multiple polypeptide chains/subunits, all bond types.

Protein Structure

Overall 3-dimensional structure of a protein is determined by the interactions of R-groups, including Van der Waals forces.

Protein Conformation

Final folded protein structure.

Chaperone Proteins

Specialized proteins that facilitate correct protein folding without dictating it; they increase the efficiency of proper folding by binding to hydrophobic regions.

Protein Structures

Form rings, filaments, sheets, and spheres; structure determines function.

Amyloid Structures

Stacks of beta-sheets in long rows that form when proteins misfold, damaging cells and tissues.

Prions

Misfolded proteins that convert properly folded proteins to a misfolded conformation, spreading through contaminated sources.

Protein Domain

Region of a protein that attaches to a substrate or another protein.

Disulfide Bonds

Covalent bonds between cysteine side chains that stabilize extracellular proteins.

Ligands

Molecules that bind specifically to proteins.

Enzymes

Bind specific substrates in the active site and speed up chemical reactions by lowering activation energy.

Protein Helpers

Small molecules that aid proteins, such as heme groups in hemoglobin and coenzymes (vitamins).

Protein Kinases

Enzymes that phosphorylate other proteins by attaching a phosphate group to an amino acid side chain, affecting protein shape and ligand binding.

Protein Synthesize

Process by which proteins are synthesized from mRNA using ribosomes as the machinery.

Allosteric Regulation

Regulation of protein activity through the binding of a molecule to a site other than the active site, changing the protein's shape and function.

Proteasomes

Large protein complexes that degrade unneeded or damaged proteins by proteolysis.