BPK 110 Final Review (updated) questions n
answers
1. Differentiate
Complete proteins: Have all nine essential amino
be- tween
acids. Ex. Animal sources of protein (milk, meat)
complete and
incomplete Incomplete proteins: Lack one or more of the essential amino
proteins and acids. Ex. Plant sources of proteins (legumes)
provide
typical
sources of
each.
2. Describe the mol- Proteins are composed of long chains of amino acids folded into very
specific pat-
ecular structure peptide bond, polypep- tide.
of proteins
and the four 4. Where/how does protein digestion occur in
lev- the body? Include key enzymes in- volved
els of protein in the
structure.
Which bonds
are essen- tial
to each level
of
organization?
3. Define the
key words:
Denatu-
ration,
deami-
nation,
, BPK 110 Final Review (updated) questions n
answers
rns. Amino acids are linked
Deamination: The removal of the nitrogen group found on proteins
together by peptide bonds
to form polypeptides.
1. In the mouth, chewing begins the mechanical breakdown of
Primary Structure: protein.
2. In the stomach, hydrochloric acid and the enzyme pepsin begin
Polypeptide chain; peptide
the chemical digestion of protein.
3. In the small intestine, pancreatic proteases (trypsin and
bonds.
chymotrypsin), along with enzymes in the microvilli break down
condary Structure: Alpha polypeptides into amino acids, dipep- tides, and tripeptides.
helices and beta-pleated
sheets; hydrogen bonds
between side chains in
the polypeptide chains.
rtiary Structure: Disulphide,
hydrogen bonds between
side chains. Quaternary
Structure: The binding of
two or more polypeptide
chains together.
enaturation: Refers to the
alteration of a protein's 3D
structure (from heat, acid,
oking, etc.)
,BPK 110 Final Review (updated) questions n
answers
process and their
source organs.
5. What risk is there Similar amino acids sometimes use the same transporter, so if there
is an over- in consuming iso- abundance of one amino acid, it may block the absorption
of another (deficiency). lates of single
amino acids?
6. Outline the high protein diet.
key functions
of pro- teins.
Use specif- ic
examples.
7. Differentiate
be- tween
kwash- iorkor
and
marasmus.
8. Contrast the
po- tential
benefits and
risks of con-
suming a
, BPK 110 Final Review (updated) questions n
answers
1. Structure: Protein Marasmus: Protein and energy deficiency leading to the depletion of fat
forms some of the base stores and wasting of muscle
structure of bone,
ligaments, mus- cles, hair, Benefits:
and skin -May be associated with weight loss
2. Enzymes: Proteins that -Can help build muscle mass
speed of the rate of
chemical reactions Risks:
3. Transport: The -Can lead to dehydration, since deamination requires more water
hemoglobin protein in excretion
blood binds to oxygen -May increase calcium loss
and allows it to be -May increase risk of kidney stones
transported by red blood
cells
4. Protection from
disease: Antibodies are
proteins that help fight ott
infection
5. Movement: Actin and
myosin are proteins that
allow muscles to contract
6. Fluid balance:
Proteins found in blood
draw in water,
reducing chance of
edema
7. Energy extraction
Kwashiorkor: Protein
deficiency leading to fluid
accumulation in the
abdomen, and a fatty liver
answers
1. Differentiate
Complete proteins: Have all nine essential amino
be- tween
acids. Ex. Animal sources of protein (milk, meat)
complete and
incomplete Incomplete proteins: Lack one or more of the essential amino
proteins and acids. Ex. Plant sources of proteins (legumes)
provide
typical
sources of
each.
2. Describe the mol- Proteins are composed of long chains of amino acids folded into very
specific pat-
ecular structure peptide bond, polypep- tide.
of proteins
and the four 4. Where/how does protein digestion occur in
lev- the body? Include key enzymes in- volved
els of protein in the
structure.
Which bonds
are essen- tial
to each level
of
organization?
3. Define the
key words:
Denatu-
ration,
deami-
nation,
, BPK 110 Final Review (updated) questions n
answers
rns. Amino acids are linked
Deamination: The removal of the nitrogen group found on proteins
together by peptide bonds
to form polypeptides.
1. In the mouth, chewing begins the mechanical breakdown of
Primary Structure: protein.
2. In the stomach, hydrochloric acid and the enzyme pepsin begin
Polypeptide chain; peptide
the chemical digestion of protein.
3. In the small intestine, pancreatic proteases (trypsin and
bonds.
chymotrypsin), along with enzymes in the microvilli break down
condary Structure: Alpha polypeptides into amino acids, dipep- tides, and tripeptides.
helices and beta-pleated
sheets; hydrogen bonds
between side chains in
the polypeptide chains.
rtiary Structure: Disulphide,
hydrogen bonds between
side chains. Quaternary
Structure: The binding of
two or more polypeptide
chains together.
enaturation: Refers to the
alteration of a protein's 3D
structure (from heat, acid,
oking, etc.)
,BPK 110 Final Review (updated) questions n
answers
process and their
source organs.
5. What risk is there Similar amino acids sometimes use the same transporter, so if there
is an over- in consuming iso- abundance of one amino acid, it may block the absorption
of another (deficiency). lates of single
amino acids?
6. Outline the high protein diet.
key functions
of pro- teins.
Use specif- ic
examples.
7. Differentiate
be- tween
kwash- iorkor
and
marasmus.
8. Contrast the
po- tential
benefits and
risks of con-
suming a
, BPK 110 Final Review (updated) questions n
answers
1. Structure: Protein Marasmus: Protein and energy deficiency leading to the depletion of fat
forms some of the base stores and wasting of muscle
structure of bone,
ligaments, mus- cles, hair, Benefits:
and skin -May be associated with weight loss
2. Enzymes: Proteins that -Can help build muscle mass
speed of the rate of
chemical reactions Risks:
3. Transport: The -Can lead to dehydration, since deamination requires more water
hemoglobin protein in excretion
blood binds to oxygen -May increase calcium loss
and allows it to be -May increase risk of kidney stones
transported by red blood
cells
4. Protection from
disease: Antibodies are
proteins that help fight ott
infection
5. Movement: Actin and
myosin are proteins that
allow muscles to contract
6. Fluid balance:
Proteins found in blood
draw in water,
reducing chance of
edema
7. Energy extraction
Kwashiorkor: Protein
deficiency leading to fluid
accumulation in the
abdomen, and a fatty liver
