- Competitive inhibitors permanently alter the enzyme, non-competitive inhibitors do not.
- Competitive inhibitors bind at the active site, non-competitive inhibitors bind elsewhere.
- Competitive inhibitors increase enzyme activity, non-competitive inhibitors decrease it.
- Competitive inhibitors are irreversible, non-competitive inhibitors are reversible.
Category: Chemistry
- Catalyze reactions at high speed.
- Store and transmit genetic information.
- Provide structural support to cells.
- Regulate metabolic pathways directly.
- Peptide bonds.
- Hydrogen bonds between backbone atoms only.
- Disulfide bridges, hydrogen bonds, ionic bonds, and hydrophobic interactions involving R-groups.
- Phosphodiester bonds.
- Molecular weight.
- Amino acid sequence.
- Chemical composition after hydrolysis.
- Biological function.
- Are consumed in the reactions they catalyze.
- Allow reactions to occur at physiological temperatures and pH by lowering activation energy.
- Make non-spontaneous reactions spontaneous.
- Increase the energy yield of reactions.
- Hydrogen bond.
- Ionic bond.
- Disulfide bond (covalent).
- Peptide bond.
- The primary sequence of the protein.
- The amino acid composition.
- A specific additional function or property of the protein.
- The protein's solubility in nonpolar solvents.
- Globular, compact shape.
- Extended, elongated structure that provides strength.
- Ability to transport oxygen.
- Catalytic activity.
- Enhanced biological activity.
- Degradation or aggregation, potentially causing disease.
- Increased solubility.
- Formation of additional peptide bonds.
- Their flexible single-chain structure.
- The constant region of the antibody.
- The unique three-dimensional shape of their variable regions (antigen-binding sites).
- Their ability to denature upon antigen binding.
- Its molecular weight.
- Its half-life in the cell.
- Its biological activity or function.
- Its density.
- Covalent bonds between R-groups.
- Extensive hydrogen bonding within the polypeptide backbone.
- Hydrophobic interactions.
- Ionic bonds between distant amino acids.
- Peptide bonds.
- Alpha-carbon atoms.
- R-groups (side chains).
- Amino groups.
- Quaternary structure.
- Primary structure.
- Molecular weight.
- Solubility.
- Carbohydrates.
- Proteins.
- Lipids.
- Nucleic acids.
- Irreversibly binds the substrate.
- Allows the enzyme to be consumed in the reaction.
- Orients the substrate correctly and stabilizes the transition state.
- Reduces the temperature of the reaction.
- Denaturation by heat.
- Binding of a competitive inhibitor.
- Proteolytic cleavage (removal of a peptide segment) to expose the active site.
- Addition of a prosthetic group.
- Hyperglycemia.
- Bone density increase.
- Impaired immune function.
- Enhanced cognitive development.
- Primary structure.
- Secondary structure.
- Tertiary structure.
- Quaternary structure.
