- 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.
No category found.
- Always active enzymes.
- Formed by partial breakdown or modification of native proteins.
- Always conjugated proteins.
- Found exclusively in the nucleus.
- Secondary structure.
- Primary structure.
- Tertiary structure.
- Quaternary structure.
- Structural protein.
- Hormonal protein.
- Transport protein.
- Storage protein.
- Simpler folding patterns.
- The formation of larger, more complex functional units with cooperative binding properties.
- Reduced stability of the protein.
- Easier denaturation.
- 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.
- Hydrolysis.
- Redox reaction.
- Dehydration synthesis.
- Isomerization.
- Water.
- Sugars.
- A non-protein prosthetic group.
- Fatty acids.
- Structural support.
- Genetic information storage.
- Energy storage.
- Catalysis.
- Primary structure.
- Amino acid sequence.
- Native three-dimensional conformation and biological activity.
- Peptide bonds.
- Provide all the necessary energy for life.
- Are the fundamental building blocks and functional components of living cells.
- Are only found in animals.
- Are always soluble in water.
- Hemoglobin.
- Actin.
- Insulin.
- Antibodies.
- Binding indiscriminately to any foreign substance.
- Possessing a highly variable binding site that perfectly complements a specific antigen.
- Being denatured by the presence of antigens.
- Transporting antigens out of the body.
- They are rapidly degraded by the body.
- The body cannot synthesize them from other precursors.
- They are only needed in very small amounts.
- They provide all the necessary energy for metabolism.
- Rigidity.
- Dynamic nature and flexibility upon substrate binding.
- Lack of specificity.
- Inability to change shape.
- Lipids.
- Carbohydrates.
- Proteins (specifically those with disulfide bonds).
- Nucleic acids.
- Hydrogen bonds.
- Peptide bonds.
- Hydrophobic interactions.
- Disulfide bridges.
- Increased energy demands.
- Higher requirement for essential amino acids for tissue synthesis and growth.
- Greater need for water absorption.
- Increased fat storage.
