- 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.
Category: Chemistry
- 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.
- Transport oxygen.
- Regulate blood glucose levels.
- Build muscle mass.
- Fight infections.
- Their high content of alpha-helices.
- Their triple-helical structure, forming strong fibers.
- Their globular, compact shape.
- Their ability to denature easily.
- 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.
- Allosteric regulation.
- Structural hierarchy.
- Enzyme specificity.
- Molecular recognition.
- Readily available glucose for energy.
- Essential building blocks for growth, repair, and synthesis of various biological molecules.
- Fiber for digestive health.
- Protective waxes and oils.
- Specificity.
- Allosteric regulation.
- Denaturation.
- Feedback inhibition.
- It is required for protein synthesis but cannot be made by the body.
- It is not required for protein synthesis in humans.
- It can be synthesized by the human body from other molecules.
- It is only found in animal products.
- Non-competitive inhibitor.
- Allosteric activator.
- Competitive inhibitor.
- Coenzyme.
- The temperature is at its optimum.
- The pH is at its optimum.
- All active sites of the enzyme molecules are saturated with substrate.
- The enzyme concentration is minimal.
- Increased metabolic rate leading to exhaustion.
- Denaturation of essential enzymes and other proteins.
- Increased oxygen demand by tissues.
- Fluid loss and dehydration.
