- Tertiary structure.
- Quaternary structure.
- Primary structure.
- Secondary structure.
Category: Chemistry
- Primary.
- Secondary.
- Tertiary.
- Quaternary.
- Are larger than their substrates.
- Can function at any temperature.
- Provide a specific microenvironment (active site) that facilitates the reaction.
- Are consumed in the reaction.
- Energy storage.
- Structural components, forming the bilayer.
- Acting as enzymes.
- Genetic information storage.
- The highest possible kinetic energy of the molecules without causing denaturation.
- Complete denaturation of the enzyme.
- Lowest possible activation energy.
- Reduced substrate concentration.
- The central alpha-carbon.
- The amino group.
- The carboxyl group.
- The unique R-group (side chain).
- Simple proteins from globular proteins.
- Fibrous proteins from simple proteins.
- Conjugated proteins from simple proteins.
- Derived proteins from conjugated proteins.
- Decreased reaction rate.
- Increased activation energy.
- Increased frequency of enzyme-substrate collisions.
- Decreased enzyme specificity.
- Monosaccharide.
- Nucleotide.
- Amino acid.
- Fatty acid.
- Catalyze a wide range of reactions.
- Bind to and act upon only one or a very limited number of substrates.
- Function at any temperature or pH.
- Be synthesized rapidly by the cell.
- The primary structure is broken.
- The amino acid sequence is altered.
- The protein refolds into a random, non-functional shape that is difficult to reverse.
- The protein gets completely hydrolyzed.
- Structural protein.
- Transport protein.
- Hormonal protein.
- Storage protein.
- They are rapidly consumed outside these ranges.
- Their three-dimensional active site structure is maintained within these ranges, but distorted outside.
- They cannot bind to substrates outside these ranges.
- Their rate of synthesis is highest in these ranges.
- Hydrolysis.
- Condensation/Dehydration synthesis.
- Oxidation.
- Reduction.
- Breaking peptide bonds.
- Interfering with hydrophobic and ionic interactions.
- Inducing new disulfide bonds.
- Changing the amino acid sequence.
- Proteins store genetic information, nucleic acids are structural.
- Proteins are polymers of amino acids, nucleic acids are polymers of nucleotides.
- Proteins contain phosphorus, nucleic acids do not.
- Proteins are only found in the nucleus, nucleic acids are found in the cytoplasm.
- Primary structure.
- Amino acid composition.
- Biological activity.
- Molecular weight.
- Molecular weight.
- Optimal pH.
- Specific three-dimensional shape.
- Amino acid quantity.
- Physical shape (fibrous/globular).
- Functional role (enzyme/hormone).
- Chemical composition and complexity.
- Solubility properties.
