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Questions and Answers
What is the primary role of using an enzyme in protein breakdown?
Which type of bond is the strongest in a protein?
What is the term for the interactions between multiple polypeptides in a protein?
What is the function of glycogen in animals?
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What is the term for organic molecules that carry specific chemical groups and assist in enzymatic reactions?
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What happens to the reaction rate at high substrate concentrations?
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What is the effect of competitive inhibitors on Km?
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Which of the following amino acids is achiral and optically inactive?
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What is the effect of proline on an alpha helix protein structure?
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What describes the linear sequence of amino acids stabilized by peptide bonds?
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Study Notes
Enzyme Structure and Function
- Enzymes are proteins that catalyze biochemical reactions, and their kinetics involve studying the rates at which they catalyze reactions.
- Irreversible inhibitors permanently deactivate enzymes, reducing effective enzyme concentration and Vmax.
- At low substrate concentrations, the reaction rate increases linearly with substrate concentration due to available enzyme active sites.
- At high substrate concentrations, the reaction rate approaches Vmax as all enzyme active sites become saturated with substrate.
- Km value reflects the enzyme's affinity for its substrate, with lower Km indicating higher substrate affinity.
- Competitive inhibitors increase Km, while noncompetitive inhibitors do not affect Km.
- Cooperativity occurs when substrate binding facilitates the binding of more substrates.
Amino Acids
- Serine (S), threonine (T), and tyrosine (Y) residues are often phosphorylated by kinases.
- Glycine is achiral and optically inactive, and can disrupt alpha helices due to its small size and flexibility.
- Proline disrupts alpha helices due to its inflexible secondary alpha-amino group.
- Cysteine forms disulfide bridges and has an R absolute configuration.
- Amino acids have different charges at different pH levels due to approximate pKa values for carboxylic acid (2) and amino groups (9).
- Neutral polar amino acids contain OH, S, or amide groups, while neutral non-polar amino acids have uncharged alkyl or aromatic side chains.
Protein Structure
- Primary structure describes the linear sequence of amino acids stabilized by peptide bonds.
- Secondary structure involves folding of a polypeptide into alpha helices and beta-pleated sheets due to backbone interactions.
- Tertiary structure is the further folding of a polypeptide due to R-group interactions, which can be disrupted by changing the pH surrounding the protein.
- Quaternary structure consists of the interactions between multiple polypeptides, and is also disrupted by pH changes.
- Disulfide bonds are found in the extracellular space and are affected by denaturation.
Cofactors and Coenzymes
- Cofactors can be inorganic ions or organic molecules, while coenzymes specifically refer to organic molecules carrying specific chemical groups.
- Cooperativity occurs when substrate binding facilitates further substrate binding, and is not explained by Michaelis-Menten kinetics.
Carbohydrates: Structure and Function
- Monosaccharides are simple sugars that serve as building blocks for more complex carbohydrates and are key energy sources in cellular respiration.
- Disaccharides include maltose, sucrose, lactose, and cellobiose.
- Polysaccharides include glycogen (energy storage in animals), starch (energy storage in plants), and cellulose (structural component in plant cell walls).
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Description
Learn about enzymes, proteins that catalyze biochemical reactions, and explore enzyme kinetics, inhibitors, and reaction rates. Understand how substrate concentration affects reaction rates.