- 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.
Author: ETEA MCQS.COM
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- 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.
- Hydrogen bond formation.
- Disulfide bridge formation.
- The overall three-dimensional folding.
- Subunit assembly.
- Fibrinogen.
- Casein.
- Metaproteins.
- Hemoglobin.
- Redox reactions.
- Condensation reactions.
- Hydrolysis reactions.
- Isomerization reactions.
- On the surface of soluble proteins in the cytoplasm.
- Embedded within cell membranes.
- In the active site of a hydrolytic enzyme.
- As a hormonal signaling molecule.
- Be easily broken down for energy.
- Achieve specific and highly diverse functions through precise 3D arrangements.
- Dissolve in any solvent.
- Avoid denaturation in any condition.
- R-groups of amino acids.
- The peptide backbone atoms.
- Different polypeptide chains.
- Amino acids and prosthetic groups.
- They are polymers formed from smaller monomeric units.
- They are typically very large molecules.
- They are all soluble in nonpolar solvents.
- Their structure dictates their function.
- Specificity.
- Optimal temperature.
- Catalytic efficiency (lowering activation energy).
- Stability to denaturation.
- Glycosidic bonds.
- Ester bonds.
- Peptide bonds.
- Phosphodiester bonds.
