- Zymogen.
- Holoenzyme.
- Prosthetic group.
- Allosteric enzyme.
Category: Chemistry
- Kwashiorkor is characterized by severe emaciation due to overall calorie deficit.
- Marasmus is mainly characterized by edema and skin lesions.
- Both Kwashiorkor and Marasmus involve inadequate protein intake, but Marasmus additionally involves inadequate total calorie intake.
- Protein deficiency only affects muscle tissue.
- Functional classification.
- Structural classification.
- Nutritional classification.
- Genetic classification.
- Increasing the frequency of collisions between reactant molecules.
- Providing an alternative reaction pathway with a lower activation energy.
- Increasing the kinetic energy of the reactants.
- Shifting the chemical equilibrium towards the product side.
- Primary structure.
- Secondary structure.
- Tertiary structure.
- Quaternary structure.
- Stabilize the primary structure.
- Connect amino acids within the backbone.
- Provide covalent cross-links that stabilize tertiary and quaternary structures.
- Form alpha-helices.
- Proteins.
- Lipids.
- Nucleic acids.
- Carbohydrates.
- All essential amino acids in sufficient quantities.
- Only non-essential amino acids.
- High levels of carbohydrates.
- Only animal-based proteins.
- Primary structure.
- Covalent bonds.
- Hydrogen bonds, ionic bonds, and hydrophobic interactions.
- Amino acid sequence.
- Transport protein.
- Structural protein.
- Hormonal protein.
- Enzymatic protein.
- The enzyme is denatured.
- All active sites on the enzyme molecules are saturated with substrate.
- The substrate concentration is too low for the enzyme to function.
- The enzyme activity decreases due to product accumulation.
- Simple proteins.
- Derived proteins.
- Conjugated proteins.
- Fibrous proteins.
- Increasing the temperature of the reactants.
- Lowering the activation energy required for the reaction to proceed.
- Changing the concentration of products.
- Making endergonic reactions exergonic.
- Secondary structure.
- Primary structure.
- Tertiary structure.
- Quaternary structure.
- Always active enzymes.
- Formed by partial breakdown or modification of native proteins.
- Always conjugated proteins.
- Found exclusively in the nucleus.
- Simpler folding patterns.
- The formation of larger, more complex functional units with cooperative binding properties.
- Reduced stability of the protein.
- Easier denaturation.
- Structural protein.
- Hormonal protein.
- Transport protein.
- Storage protein.
- It has the highest kinetic energy possible.
- Its active site is in the most favorable conformation for substrate binding and catalysis.
- All enzyme molecules are fully denatured.
- It undergoes continuous synthesis.
- Fatty acids.
- Amino acids.
- Glucose molecules.
- Nucleotides.
