Biochemistry Exam Questions
and Answers 100% PASS
Amino Acids—ANSWER-Have an amino group, carboxylic acid, hydrogen
atom, and an R group attached to a central α-carbon
Amino Acid Structure—ANSWER-1. Chiral (L) except for glycine, and have
the (S) configuration, except for cysteine.
2. Side Chains determine the chemistry and function of amino acids.
Nonpolar, nonaromatic—ANSWER-Glycine, Alanine, Valine, Leucine,
Isoleucine, Methionine, and Proline
Aromatic—ANSWER-Tryptophan, Phenylalanine, and Tyrosine
Polar—ANSWER-Serine, Theronine, Asparagine, Glutamine, and Cysteine
Negatively Charged (Acidic)—ANSWER-Aspartic Acid and Glutamic Acid
Positively Charged (Basic)—ANSWER-Lysine, Arginine, and Histidine
Amino Acid Chemistry—ANSWER--Amphoteric
-Protonated at low pH
-Zwitterion at neutral pH
-Fully deprotonated at high pH
, pL—ANSWER-Determine by averaging pKa values that refer to protonation
and deprotonation of the zwitterion
Peptide Bonds—ANSWER-Formed through condensation (dehydration)
reaction with a nucleophilic amino group attacking an electrophilic
carbonyl. Broken through hydrolysis.
Protein Structure—ANSWER-Primary, Secondary, Tertiary, and Quaternary
Primary Structure—ANSWER-Linear sequence of amino acids
Secondary Structure—ANSWER-Local structure, stabilized by hydrogen
bonding:
α-helices and β-pleated sheets
Tertiary Structure—ANSWER-Three-dimensional structure stabilized by
hydrophobic interactions, acid-base interactions (salt bridges), hydrogen
bonding, and disulfide bonds
Quaternary Structure—ANSWER-Interactions between subunits, heat and
solutes cause denaturation
Structural Proteins—ANSWER-Generally fibrous, include collagen, elastin,
keratin, actin, and tubulin
Motor Proteins—ANSWER-Capable of force generation through a
conformational change. Include myosin, kinesin, and dyenin
Binding Proteins—ANSWER-Bind a specific substrate, either to sequester it
in the body or hold its concentration at a steady state
© 2026 Copyright. All Rights Reserved. This document is
protected by copyright law
and Answers 100% PASS
Amino Acids—ANSWER-Have an amino group, carboxylic acid, hydrogen
atom, and an R group attached to a central α-carbon
Amino Acid Structure—ANSWER-1. Chiral (L) except for glycine, and have
the (S) configuration, except for cysteine.
2. Side Chains determine the chemistry and function of amino acids.
Nonpolar, nonaromatic—ANSWER-Glycine, Alanine, Valine, Leucine,
Isoleucine, Methionine, and Proline
Aromatic—ANSWER-Tryptophan, Phenylalanine, and Tyrosine
Polar—ANSWER-Serine, Theronine, Asparagine, Glutamine, and Cysteine
Negatively Charged (Acidic)—ANSWER-Aspartic Acid and Glutamic Acid
Positively Charged (Basic)—ANSWER-Lysine, Arginine, and Histidine
Amino Acid Chemistry—ANSWER--Amphoteric
-Protonated at low pH
-Zwitterion at neutral pH
-Fully deprotonated at high pH
, pL—ANSWER-Determine by averaging pKa values that refer to protonation
and deprotonation of the zwitterion
Peptide Bonds—ANSWER-Formed through condensation (dehydration)
reaction with a nucleophilic amino group attacking an electrophilic
carbonyl. Broken through hydrolysis.
Protein Structure—ANSWER-Primary, Secondary, Tertiary, and Quaternary
Primary Structure—ANSWER-Linear sequence of amino acids
Secondary Structure—ANSWER-Local structure, stabilized by hydrogen
bonding:
α-helices and β-pleated sheets
Tertiary Structure—ANSWER-Three-dimensional structure stabilized by
hydrophobic interactions, acid-base interactions (salt bridges), hydrogen
bonding, and disulfide bonds
Quaternary Structure—ANSWER-Interactions between subunits, heat and
solutes cause denaturation
Structural Proteins—ANSWER-Generally fibrous, include collagen, elastin,
keratin, actin, and tubulin
Motor Proteins—ANSWER-Capable of force generation through a
conformational change. Include myosin, kinesin, and dyenin
Binding Proteins—ANSWER-Bind a specific substrate, either to sequester it
in the body or hold its concentration at a steady state
© 2026 Copyright. All Rights Reserved. This document is
protected by copyright law
