- Allosteric regulation.
- Structural hierarchy.
- Enzyme specificity.
- Molecular recognition.
Category: Macro Mulecule
- 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.
- Glycosidic bonds and ester linkages.
- Peptide bonds and phosphodiester bonds.
- Hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges.
- Amide bonds and peptide bonds only.
- Collagen.
- Keratin.
- Hemoglobin.
- Insulin.
- Amino group of one amino acid and the R-group of another.
- Carboxyl group of one amino acid and the amino group of another.
- R-groups of two adjacent amino acids.
- Carbonyl oxygen of one and the hydrogen of another.
- Independent polypeptide chains in a multimeric protein.
- Regions of a protein that fold independently and often have specific functions.
- Localized areas of alpha-helices and beta-sheets.
- The entire three-dimensional structure of a protein.
- Energy storage.
- Muscle contraction.
- Cell-cell recognition and signaling.
- Oxygen transport.
- Genetic information storage.
- Long-term energy storage and structural support.
- Catalysis of biochemical reactions.
- Cellular signaling.
- Slight changes in temperature within its optimal range.
- Binding of a competitive inhibitor.
- Extreme changes in pH or temperature, leading to permanent disruption of its active site.
- Short-term exposure to high substrate concentration.
- Denature most other enzymes.
- Inhibit all protein activity.
- Promote strong hydrogen bonding.
- Lead to polymerization of substrates.
- Primary only.
- Secondary only.
- Tertiary and quaternary.
- Primary and secondary.
- Carbohydrates.
- Lipids.
- Proteins.
- Nucleic acids.
