BioChem 210 Final Exam - Portage Learning
Question and Answer | Updated Verified
Answers | Study Guide Pack
• ΔG -✓✓Gibbs free energy; negative = spontaneous, positive = non-spontaneous.
• Central Dogma -✓✓DNA → RNA → Protein.
• Classes of Biomolecules -✓✓Carbohydrates, lipids, proteins, nucleic acids.
• Water as a biological solvent -✓✓Dissolves polar and charged molecules using
hydration shells.
• Polar Molecules -✓✓Unequal electron sharing; dissolve in water.
• Nonpolar Molecules -✓✓Equal electron sharing; hydrophobic.
• Hydrogen Bonding -✓✓Weak attraction between hydrogen and electronegative atoms
like O or N.
• Van Der Wal forces -✓✓Weak, transient dipole interactions.
• Buffering system -✓✓Weak acid/conjugate base resisting pH change.
• Henderson-Hasselbalch equation -✓✓
• pKa on titration curve -✓✓midpoint of buffering region
• Isoelectric Point (Ip) -✓✓pH at which amino acid has net charge of zero.
• Hydrophobic effect -✓✓Nonpolar molecules cluster to reduce water ordering.
• Essential amino acids -✓✓Must be consumed through diet.
• Non-essential amino acids -✓✓Produced by the body.
• Peptide bond -✓✓Amide bond between COOH and NH₂ formed by dehydration.
• Primary structure -✓✓Amino acid sequence.
• Secondary structure -✓✓α-helix and β-sheet.
, • Tertiary structures -✓✓3D folding of a polypeptide chain.
• quatenary structure -✓✓Association of multiple polypeptide subunits.
• Forces in Protien structure -✓✓Hydrogen bonds, ionic bonds, disulfide bonds,
hydrophobic interactions, Van der Waals.
• Protein Denaturation -✓✓Loss of structure from heat, pH, or chemicals.
• Hemoglobin function -✓✓O₂ transport; sigmoidal binding curve.
• Myoglobin function -✓✓O₂ storage; hyperbolic binding curve.
• Enzyme properties -✓✓Catalysts that lower activation energy and increase reaction
rate
• Michaelis-Menten Equation -✓✓
• Km -✓✓Substrate concentration at ½ Vmax; measures affinity.
• Vmax -✓✓maximum enzyme rate
• kcat (turnover number) -✓✓Substrates converted to product per enzyme per second.
• Competitive Inhibition -✓✓Binds active site; increases Km, Vmax unchanged.
• Noncompetitive Inhibition -✓✓Binds allosteric site; decreases Vmax, Km unchanged.
• Uncompetitive Inhibition -✓✓Decreases Km and Vmax.
• Chymotrypsin Mechanism -✓✓Ser-His-Asp catalytic triad cleaves peptide bonds.
• aldose -✓✓Monosaccharide with aldehyde group.
• ketose -✓✓Monosaccharide with ketone group.
• α-Glycosidic Linkage -✓✓OH on anomeric carbon points down.
• β-Glycosidic Linkage -✓✓OH on anomeric carbon points up.
• Reducing End -✓✓Sugar end with free anomeric carbon.
Question and Answer | Updated Verified
Answers | Study Guide Pack
• ΔG -✓✓Gibbs free energy; negative = spontaneous, positive = non-spontaneous.
• Central Dogma -✓✓DNA → RNA → Protein.
• Classes of Biomolecules -✓✓Carbohydrates, lipids, proteins, nucleic acids.
• Water as a biological solvent -✓✓Dissolves polar and charged molecules using
hydration shells.
• Polar Molecules -✓✓Unequal electron sharing; dissolve in water.
• Nonpolar Molecules -✓✓Equal electron sharing; hydrophobic.
• Hydrogen Bonding -✓✓Weak attraction between hydrogen and electronegative atoms
like O or N.
• Van Der Wal forces -✓✓Weak, transient dipole interactions.
• Buffering system -✓✓Weak acid/conjugate base resisting pH change.
• Henderson-Hasselbalch equation -✓✓
• pKa on titration curve -✓✓midpoint of buffering region
• Isoelectric Point (Ip) -✓✓pH at which amino acid has net charge of zero.
• Hydrophobic effect -✓✓Nonpolar molecules cluster to reduce water ordering.
• Essential amino acids -✓✓Must be consumed through diet.
• Non-essential amino acids -✓✓Produced by the body.
• Peptide bond -✓✓Amide bond between COOH and NH₂ formed by dehydration.
• Primary structure -✓✓Amino acid sequence.
• Secondary structure -✓✓α-helix and β-sheet.
, • Tertiary structures -✓✓3D folding of a polypeptide chain.
• quatenary structure -✓✓Association of multiple polypeptide subunits.
• Forces in Protien structure -✓✓Hydrogen bonds, ionic bonds, disulfide bonds,
hydrophobic interactions, Van der Waals.
• Protein Denaturation -✓✓Loss of structure from heat, pH, or chemicals.
• Hemoglobin function -✓✓O₂ transport; sigmoidal binding curve.
• Myoglobin function -✓✓O₂ storage; hyperbolic binding curve.
• Enzyme properties -✓✓Catalysts that lower activation energy and increase reaction
rate
• Michaelis-Menten Equation -✓✓
• Km -✓✓Substrate concentration at ½ Vmax; measures affinity.
• Vmax -✓✓maximum enzyme rate
• kcat (turnover number) -✓✓Substrates converted to product per enzyme per second.
• Competitive Inhibition -✓✓Binds active site; increases Km, Vmax unchanged.
• Noncompetitive Inhibition -✓✓Binds allosteric site; decreases Vmax, Km unchanged.
• Uncompetitive Inhibition -✓✓Decreases Km and Vmax.
• Chymotrypsin Mechanism -✓✓Ser-His-Asp catalytic triad cleaves peptide bonds.
• aldose -✓✓Monosaccharide with aldehyde group.
• ketose -✓✓Monosaccharide with ketone group.
• α-Glycosidic Linkage -✓✓OH on anomeric carbon points down.
• β-Glycosidic Linkage -✓✓OH on anomeric carbon points up.
• Reducing End -✓✓Sugar end with free anomeric carbon.
