- Increased metabolic rate leading to exhaustion.
- Denaturation of essential enzymes and other proteins.
- Increased oxygen demand by tissues.
- Fluid loss and dehydration.
Category: Chemistry
- 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.
- 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.
- 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.
- 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.
- Transfer RNA (tRNA).
- Ribosomal RNA (rRNA).
- Messenger RNA (mRNA).
- Aminoacyl-tRNA synthetase.
- Carbohydrates.
- Lipids.
- Proteins.
- Nucleic acids.
- Hydrophobic interactions burying nonpolar R-groups in the interior and hydrophilic interactions exposing polar R-groups on the surface.
- Extensive disulfide bonds throughout the entire structure.
- Continuous alpha-helix formation.
- The rigid backbone structure.
- Peptide bonds.
- Glycosidic bonds.
- Hydrogen bonds, ionic bonds, and hydrophobic interactions.
- Phosphodiester bonds.
- Structural components.
- Transport agents.
- Highly specific biocatalysts (enzymes).
- Hormonal regulators.
- Nucleic acid structure.
- Carbohydrate branching.
- Protein folding and function.
- Lipid bilayer formation.
