WGU C785 BIOCHEMISTRY MODULE 2
carboxyl group - ✔A -COOH group, found in organic acids.
amino group - ✔a chemical group consisting of a nitrogen atom bonded to two
hydrogen atoms
Where are the hydrophobic amino acids found in the protein? - ✔found in the interior of
the protein
What kind of bond connects a positively charged group and a negatively charged
group? - ✔ionic bond
What type of reaction forms a peptide bond? - ✔dehydration synthesis
What type of reactions breaks the peptide bond? - ✔Hydrolysis reaction
Peptide bonds are in what structure? - ✔Primary structure
Hydrogen bonds hold which structure together? - ✔Secondary and tertiary
What amino acids are found on the exterior of the protein? - ✔polar amino acids
Two non-polar amino acids make what kind of interaction? - ✔Hydrophobic interactions
Non-covalent interactions between amino acid R groups - ✔hydrophobic, ionic and
hydrogen bonds
What structure has a disulfide bond that holds together 2 subunits of an enzyme? - ✔
quaternary structure
What structure has an Ionic interactions that hold together 4 different subunits of a
protein? - ✔quaternary structure
What structure has an Ionic interactions that hold together 3 identical polypeptides - ✔
quaternary structure
non polar amino acids - ✔hydrophobic bond, weak strength, heat disrupts the
interaction
primary structure of protein - ✔the amino acid sequence of the polypeptide chain
secondary structure of protein - ✔Hydrogen bonds are involved in this level of structure
and the amino and carboxyl groups (backbone) form these bonds
, WGU C785 BIOCHEMISTRY MODULE 2
tertiary structure of protein - ✔hydrogen, ionic and disulfide bonds as well as
hydrophobic interactions. The entire three-dimensional structure of a single chain
polypeptide including the conformations of its side chains.
quaternary structure of a protein - ✔2 or more polypeptides interact to form the protein
Fate of misfolded proteins - ✔aggregation, degradation and refolding
What kind of interaction between misfolded protein leads to aggregation? - ✔
hydrophobic interaction
What kind of proteins take part in the process involving refolding? - ✔chaperones
A diabetic patient is suffering from ketoacidosis has low blood pH. What bond or
interaction is most likely to be disrupted within a patient's hemoglobin? - ✔hydrogen
bonds and ionic interactions
A patient presents with a fever of 110 F. Which bond or interactions is most likely to be
disrupted within a neuronal protein if the fever isn't resolved quickly? - ✔hydrophobic
interactions
Frying an egg in a pan changes the egg white color, due to the protein ovalbumin, from
translucent to white. Which bond or interaction is most likely to be disrupted within the
ovalbumin? - ✔hydrophobic interactions
Protein heated to 140F loss of function and denatured - ✔loss of function and
denatured
Native protein misfolds and remains misfolded loss of function and aggregated - ✔loss
of function and aggregated
Normally active protein at physiological blood pH, where placed in a solution with a very
low pH (less than 2) loss of function and denatured - ✔loss of function and denatured
Protein is placed in a solution with a very high pH (greater than 10) loss of function and
denatured - ✔loss of function and denatured
Protein is modified by adding a phosphate group either loss or no loss of function - ✔
loss or no loss of function
Composed of amino acids - ✔Proteins, enzymes, cell membrane receptors, antibodies,
DNA polymerase
Enzymes are a - ✔special type of protein, so they are also composed of amino acids
carboxyl group - ✔A -COOH group, found in organic acids.
amino group - ✔a chemical group consisting of a nitrogen atom bonded to two
hydrogen atoms
Where are the hydrophobic amino acids found in the protein? - ✔found in the interior of
the protein
What kind of bond connects a positively charged group and a negatively charged
group? - ✔ionic bond
What type of reaction forms a peptide bond? - ✔dehydration synthesis
What type of reactions breaks the peptide bond? - ✔Hydrolysis reaction
Peptide bonds are in what structure? - ✔Primary structure
Hydrogen bonds hold which structure together? - ✔Secondary and tertiary
What amino acids are found on the exterior of the protein? - ✔polar amino acids
Two non-polar amino acids make what kind of interaction? - ✔Hydrophobic interactions
Non-covalent interactions between amino acid R groups - ✔hydrophobic, ionic and
hydrogen bonds
What structure has a disulfide bond that holds together 2 subunits of an enzyme? - ✔
quaternary structure
What structure has an Ionic interactions that hold together 4 different subunits of a
protein? - ✔quaternary structure
What structure has an Ionic interactions that hold together 3 identical polypeptides - ✔
quaternary structure
non polar amino acids - ✔hydrophobic bond, weak strength, heat disrupts the
interaction
primary structure of protein - ✔the amino acid sequence of the polypeptide chain
secondary structure of protein - ✔Hydrogen bonds are involved in this level of structure
and the amino and carboxyl groups (backbone) form these bonds
, WGU C785 BIOCHEMISTRY MODULE 2
tertiary structure of protein - ✔hydrogen, ionic and disulfide bonds as well as
hydrophobic interactions. The entire three-dimensional structure of a single chain
polypeptide including the conformations of its side chains.
quaternary structure of a protein - ✔2 or more polypeptides interact to form the protein
Fate of misfolded proteins - ✔aggregation, degradation and refolding
What kind of interaction between misfolded protein leads to aggregation? - ✔
hydrophobic interaction
What kind of proteins take part in the process involving refolding? - ✔chaperones
A diabetic patient is suffering from ketoacidosis has low blood pH. What bond or
interaction is most likely to be disrupted within a patient's hemoglobin? - ✔hydrogen
bonds and ionic interactions
A patient presents with a fever of 110 F. Which bond or interactions is most likely to be
disrupted within a neuronal protein if the fever isn't resolved quickly? - ✔hydrophobic
interactions
Frying an egg in a pan changes the egg white color, due to the protein ovalbumin, from
translucent to white. Which bond or interaction is most likely to be disrupted within the
ovalbumin? - ✔hydrophobic interactions
Protein heated to 140F loss of function and denatured - ✔loss of function and
denatured
Native protein misfolds and remains misfolded loss of function and aggregated - ✔loss
of function and aggregated
Normally active protein at physiological blood pH, where placed in a solution with a very
low pH (less than 2) loss of function and denatured - ✔loss of function and denatured
Protein is placed in a solution with a very high pH (greater than 10) loss of function and
denatured - ✔loss of function and denatured
Protein is modified by adding a phosphate group either loss or no loss of function - ✔
loss or no loss of function
Composed of amino acids - ✔Proteins, enzymes, cell membrane receptors, antibodies,
DNA polymerase
Enzymes are a - ✔special type of protein, so they are also composed of amino acids
