MCB 450 Exam 1 Learning Objectives
UPDATED ACTUAL QUESTIONS AND
CORRECT ANSWERS
Know the four types of biological molecules & their general roles in Cells. - CORRECT ANSWER
Carbohydrates: Energy storage & structural support.
Lipids: Energy storage, membrane structure & signaling.
Proteins: Enzymatic activity, structural support, transport.
Nucleic Acids: Genetic information storage & transmission.
Know the properties of the four types of covalent bonds (formation, enzymes, biomolecules). What is
the condensation reaction to form the covalent bonds? - CORRECT ANSWER Peptide Bonds
(Proteins), Glycosidic Bonds (Carbohydrates), Phosphodiester Bonds (Nucleic Acids), Ester Bonds
(Lipids).
Condensation Reaction: A dehydration synthesis where water is removed to form bonds.
Understand unique feature of water as a dipolar and cohesive molecule. Know the properties of
hydrogen bond. - CORRECT ANSWER Water is dipolar, cohesive, has high heat capacity &
solvent properties.
Hydrogen bonds contribute to its unique properties & biomolecular interactions.
Know the properties of hydrophilic, hydrophobic, and amphipathic Molecules. - CORRECT
ANSWER Hydrophilic: Water-loving (polar molecules, ions).
Hydrophobic: Water-fearing (nonpolar molecules, lipids).
Amphipathic: Has both hydrophilic & hydrophobic parts (phospholids)
Understand the four types of weak, non-covalent interactions and their functions. - CORRECT
ANSWER Hydrogen Bonds, Ionic Interactions, Van der Waals Forces, Hydrophobic
Interactions.
Learn how to solve problems involving pH. - CORRECT ANSWER Use the formula pH = -
log[H⁺].
pH increases when [H⁺] decreases & vice versa.
, Understand how buffer works. - CORRECT ANSWER Buffers resist pH changes by absorbing
or donating H⁺ ions (e.g., bicarbonate buffer in blood).
Know how to use Henderson-Hasselbalch equation to make or change the pH of a buffer. -
CORRECT ANSWER Used to calculate pH, pKa, or buffer composition.
Understand how the peptide bond is formed and its planar characteristics. - CORRECT ANSWER
Peptide bonds form via a condensation reaction.
Planar due to partial double-bond character (resonance).
Understand major properties of each group of amino acids: their polarities, structural side chains and
characteristics. - CORRECT ANSWER Nonpolar, Polar Uncharged, Acidic (negatively
charged), Basic (positively charged).
Understand the various levels of protein structure & how they are related to one another. - CORRECT
ANSWER Primary (Amino Acid Sequence)
Secondary (α-helices, β-sheets)
Tertiary (3D folding due to side chains)
Quaternary (Multiple polypeptides interacting).
Why proline is called "a helix breaker"? - CORRECT ANSWER Its rigid cyclic structure
disrupts α-helices by introducing kinks.
Has a Nitrogen - causes H bonds
What is a disulfide bond? How does it contribute to protein folding? - CORRECT ANSWER
Covalent bonds between two cysteine residues, stabilizing tertiary protein structure.
Know the driving forces in protein folding or stabilization of protein Conformation. - CORRECT
ANSWER Hydrophobic interactions, Hydrogen bonding, Ionic interactions, Van der Waals
forces.
What's involved in protein denaturation? What do heat, pH and urea do in protein denaturation? -
CORRECT ANSWER Heat disrupts hydrogen bonds.
UPDATED ACTUAL QUESTIONS AND
CORRECT ANSWERS
Know the four types of biological molecules & their general roles in Cells. - CORRECT ANSWER
Carbohydrates: Energy storage & structural support.
Lipids: Energy storage, membrane structure & signaling.
Proteins: Enzymatic activity, structural support, transport.
Nucleic Acids: Genetic information storage & transmission.
Know the properties of the four types of covalent bonds (formation, enzymes, biomolecules). What is
the condensation reaction to form the covalent bonds? - CORRECT ANSWER Peptide Bonds
(Proteins), Glycosidic Bonds (Carbohydrates), Phosphodiester Bonds (Nucleic Acids), Ester Bonds
(Lipids).
Condensation Reaction: A dehydration synthesis where water is removed to form bonds.
Understand unique feature of water as a dipolar and cohesive molecule. Know the properties of
hydrogen bond. - CORRECT ANSWER Water is dipolar, cohesive, has high heat capacity &
solvent properties.
Hydrogen bonds contribute to its unique properties & biomolecular interactions.
Know the properties of hydrophilic, hydrophobic, and amphipathic Molecules. - CORRECT
ANSWER Hydrophilic: Water-loving (polar molecules, ions).
Hydrophobic: Water-fearing (nonpolar molecules, lipids).
Amphipathic: Has both hydrophilic & hydrophobic parts (phospholids)
Understand the four types of weak, non-covalent interactions and their functions. - CORRECT
ANSWER Hydrogen Bonds, Ionic Interactions, Van der Waals Forces, Hydrophobic
Interactions.
Learn how to solve problems involving pH. - CORRECT ANSWER Use the formula pH = -
log[H⁺].
pH increases when [H⁺] decreases & vice versa.
, Understand how buffer works. - CORRECT ANSWER Buffers resist pH changes by absorbing
or donating H⁺ ions (e.g., bicarbonate buffer in blood).
Know how to use Henderson-Hasselbalch equation to make or change the pH of a buffer. -
CORRECT ANSWER Used to calculate pH, pKa, or buffer composition.
Understand how the peptide bond is formed and its planar characteristics. - CORRECT ANSWER
Peptide bonds form via a condensation reaction.
Planar due to partial double-bond character (resonance).
Understand major properties of each group of amino acids: their polarities, structural side chains and
characteristics. - CORRECT ANSWER Nonpolar, Polar Uncharged, Acidic (negatively
charged), Basic (positively charged).
Understand the various levels of protein structure & how they are related to one another. - CORRECT
ANSWER Primary (Amino Acid Sequence)
Secondary (α-helices, β-sheets)
Tertiary (3D folding due to side chains)
Quaternary (Multiple polypeptides interacting).
Why proline is called "a helix breaker"? - CORRECT ANSWER Its rigid cyclic structure
disrupts α-helices by introducing kinks.
Has a Nitrogen - causes H bonds
What is a disulfide bond? How does it contribute to protein folding? - CORRECT ANSWER
Covalent bonds between two cysteine residues, stabilizing tertiary protein structure.
Know the driving forces in protein folding or stabilization of protein Conformation. - CORRECT
ANSWER Hydrophobic interactions, Hydrogen bonding, Ionic interactions, Van der Waals
forces.
What's involved in protein denaturation? What do heat, pH and urea do in protein denaturation? -
CORRECT ANSWER Heat disrupts hydrogen bonds.
