- Proteins.
- Lipids.
- Carbohydrates.
- Nucleic acids.
Category: Macro Mulecule
- 0.1-0.2 g/kg body weight.
- 0.8-1.0 g/kg body weight.
- 2.0-2.5 g/kg body weight.
- 5.0-10.0 g/kg body weight.
- Plant-based foods like fruits and vegetables.
- Complete proteins from animal sources (e.g., meat, eggs, dairy).
- Refined grains.
- Sugars and starches.
- Any region of the enzyme where an inhibitor can bind.
- The specific three-dimensional region on the enzyme where the substrate binds and catalysis occurs.
- The site where the enzyme is synthesized.
- The entire surface of the enzyme molecule.
- Allosteric regulation.
- Irreversibility.
- High specificity.
- Optimal pH.
- Substrate.
- Hormone.
- Enzyme.
- Antibody.
- Inter-chain disulfide bonds.
- Intramolecular hydrogen bonding involving the polypeptide backbone.
- Side-chain interactions.
- Quaternary arrangements.
- Hydrolysis.
- Polymerization.
- Dehydration synthesis (condensation).
- Oxidation.
- Peptide bonds by adding ions.
- Hydrophobic interactions and ionic bonds by interfering with electrostatic forces and hydration shells.
- Disulfide bridges by acting as a reducing agent.
- The primary amino acid sequence.
- Only function as structural components.
- Perform functions that amino acid side chains alone cannot achieve, such as carrying oxygen or absorbing light.
- Be easily hydrolyzed into simple amino acids.
- Maintain a rigid, unchanging structure.
- Increase the production of the end product.
- Prevent overproduction of the end product by regulating its synthesis.
- Activate alternative metabolic pathways.
- Increase the diversity of metabolic intermediates.
- Increase the temperature of the reaction.
- Form permanent bonds with the substrate.
- Lower the activation energy of the reaction.
- Shift the equilibrium of the reaction to favor product formation.
- The amino acid sequence of the active site, which allows for precise complementary fit.
- The overall size of the enzyme molecule.
- Its solubility in the reaction medium.
- Its ability to change shape indefinitely.
- Hemoglobin.
- Pepsin.
- Peptone.
- Glycoprotein.
- Their high content of alpha-helices.
- Their triple-helical structure, forming strong fibers.
- Their globular, compact shape.
- Their ability to denature easily.
- Transport oxygen.
- Regulate blood glucose levels.
- Build muscle mass.
- Fight infections.
- Its individual polypeptide chains have unfolded.
- The specific sequence of amino acids has been altered.
- The non-covalent interactions between multiple polypeptide subunits have been broken.
- The protein has formed a stable, non-functional aggregate.
- Energy storage and transfer.
- Catalysis of biochemical reactions.
- Hereditary information storage and transmission.
- Structural support.
- The substrate cannot reach the active site.
- The active site's shape and charge distribution are altered due to changes in ionization of amino acid side chains.
- The peptide bonds are broken.
- The enzyme concentration decreases.
