MCB 450 EXAM 1 [2026] UPDATED ACTUAL Exam |
Question and Answer | DETAILED SOLUTIONS &
EXAM REVIEW
• Understand unique feature of water as a dipolar and cohesive molecule. Know
the properties of hydrogen bond. -✓✓ 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. -
✓✓ 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. -✓✓ Hydrogen Bonds, Ionic Interactions, Van der Waals Forces,
Hydrophobic Interactions.
• Learn how to solve problems involving pH. -✓✓ Use the formula pH = -log[H⁺].
pH increases when [H⁺] decreases & vice versa.
• Understand how buffer works. -✓✓ 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. -✓✓ Used to calculate pH, pKa, or buffer composition.
, • Understand how the peptide bond is formed and its planar characteristics. -✓✓
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. -✓✓ Nonpolar, Polar Uncharged, Acidic
(negatively charged), Basic (positively charged).
• Understand the various levels of protein structure & how they are related to
one another. -✓✓ 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"? -✓✓ 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? -✓✓
Covalent bonds between two cysteine residues, stabilizing tertiary protein
structure.
• Know the driving forces in protein folding or stabilization of protein
Conformation. -✓✓ Hydrophobic interactions, Hydrogen bonding, Ionic
interactions, Van der Waals forces.
Question and Answer | DETAILED SOLUTIONS &
EXAM REVIEW
• Understand unique feature of water as a dipolar and cohesive molecule. Know
the properties of hydrogen bond. -✓✓ 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. -
✓✓ 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. -✓✓ Hydrogen Bonds, Ionic Interactions, Van der Waals Forces,
Hydrophobic Interactions.
• Learn how to solve problems involving pH. -✓✓ Use the formula pH = -log[H⁺].
pH increases when [H⁺] decreases & vice versa.
• Understand how buffer works. -✓✓ 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. -✓✓ Used to calculate pH, pKa, or buffer composition.
, • Understand how the peptide bond is formed and its planar characteristics. -✓✓
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. -✓✓ Nonpolar, Polar Uncharged, Acidic
(negatively charged), Basic (positively charged).
• Understand the various levels of protein structure & how they are related to
one another. -✓✓ 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"? -✓✓ 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? -✓✓
Covalent bonds between two cysteine residues, stabilizing tertiary protein
structure.
• Know the driving forces in protein folding or stabilization of protein
Conformation. -✓✓ Hydrophobic interactions, Hydrogen bonding, Ionic
interactions, Van der Waals forces.
