CHEM 210 BIOCHEMISTRY MODULE 3 EXAM
PORTAGE LEARNING 2026 COMPREHENSIVE
REVIEW PACK VERIFIED ANSWERS A+
◉ Define transport function of proteins and example. Answer: helps to
move molecules around the cell and organism, ex: Hemoglobin is a
blood-based protein that carries oxygen from the lungs to tissue
◉ Define hormone function of proteins and example. Answer:
Hormones communicate messages between cells, ex: relaxin is a protein
hormone that helps women relax pelvic ligaments during childbirth
◉ Define catalysis function of proteins and example. Answer: Enzymes
speed up or catalyze chemical rxns, ex: protease enzyme breaks down
proteins in cells to help organisms recycle unneeded proteins
◉ Define structure function of proteins and example. Answer: Proteins
give strength to cells, organelles and tissues, ex: collagen is the
structural protein in cartilage, skin and tendons
◉ Define amino acids. Answer: building blocks of proteins
◉ What functional groups do amino acids contain?. Answer: amine and
carboxylic acid
,◉ What permits all amino acids to link together in a protein?. Answer:
Each amino acid having the same groups
◉ What is the R group in an amino acid and how are they grouped?.
Answer: Side chain of the amino acid; there are 20 different side chains
that differ in composition/size/charge so side chains are grouped by
charge, size and polarity
◉ What pH do amino acids exist at?. Answer: 7.4
◉ What do amino acids lose and gain at pH of 7.4?. Answer: Lose the
carboxylic acid H group and gain an extra proton (NH3+)
◉ Name the 5 sets of amino acids. Answer: Non-polar aliphatic, non-
polar aromatic, polar neutral, acidic, basic
◉ Define non-polar aliphatic amino acids. Answer: Straight chain amino
acids
◉ Name the 7 nonpolar, aliphatic amino acids. Answer: glycine (Gly,
G), alanine (Ala, A), proline (Pro, P), valine (Val, V), leucine (Leu, L),
isoleucine (Ile, I), methionine (Met, M)
◉ Name the 7 nonpolar, aliphatic amino acids in abbreviations. Answer:
Gly, Ala, Val, Pro, Leu, Ile, Met
, ◉ Describe aliphatic amino acids and their location in proteins. Answer:
Relatively small which allows them to interact with other groups, found
in interior of protein away from water with other aliphatic groups (fold
together)
◉ Why is proline unique?. Answer: its side chain makes a ring by
bonding with its main chain nitrogen
◉ How do non-polar aromatic groups compare to aliphatic? (5 reasons).
Answer: similar to aliphatic in that they are non-polar, but the side
chains of these compounds contain a ring of carbons as an aromatic
functional group, not as small as the aliphatic, but they are more rigid,
aromatic ring structures have unique physical and chemical properties
◉ Why are the benzene rings important in aromatic groups?. Answer:
The double bonds (conjugated system) absorb light well for proteins
◉ Name the 3 non-polar aromatic groups. Answer: Phenylalanine
(Phe,F), Tryptophan (Trp,W), Tyrosine (Tyr,Y)
◉ Describe the polar neutral amino acids and location in proteins.
Answer: side chains that have a dipole, and most can hydrogen bond,
permits these amino acids to interact strongly with water, found on the
outside of the protein and in contact with water
PORTAGE LEARNING 2026 COMPREHENSIVE
REVIEW PACK VERIFIED ANSWERS A+
◉ Define transport function of proteins and example. Answer: helps to
move molecules around the cell and organism, ex: Hemoglobin is a
blood-based protein that carries oxygen from the lungs to tissue
◉ Define hormone function of proteins and example. Answer:
Hormones communicate messages between cells, ex: relaxin is a protein
hormone that helps women relax pelvic ligaments during childbirth
◉ Define catalysis function of proteins and example. Answer: Enzymes
speed up or catalyze chemical rxns, ex: protease enzyme breaks down
proteins in cells to help organisms recycle unneeded proteins
◉ Define structure function of proteins and example. Answer: Proteins
give strength to cells, organelles and tissues, ex: collagen is the
structural protein in cartilage, skin and tendons
◉ Define amino acids. Answer: building blocks of proteins
◉ What functional groups do amino acids contain?. Answer: amine and
carboxylic acid
,◉ What permits all amino acids to link together in a protein?. Answer:
Each amino acid having the same groups
◉ What is the R group in an amino acid and how are they grouped?.
Answer: Side chain of the amino acid; there are 20 different side chains
that differ in composition/size/charge so side chains are grouped by
charge, size and polarity
◉ What pH do amino acids exist at?. Answer: 7.4
◉ What do amino acids lose and gain at pH of 7.4?. Answer: Lose the
carboxylic acid H group and gain an extra proton (NH3+)
◉ Name the 5 sets of amino acids. Answer: Non-polar aliphatic, non-
polar aromatic, polar neutral, acidic, basic
◉ Define non-polar aliphatic amino acids. Answer: Straight chain amino
acids
◉ Name the 7 nonpolar, aliphatic amino acids. Answer: glycine (Gly,
G), alanine (Ala, A), proline (Pro, P), valine (Val, V), leucine (Leu, L),
isoleucine (Ile, I), methionine (Met, M)
◉ Name the 7 nonpolar, aliphatic amino acids in abbreviations. Answer:
Gly, Ala, Val, Pro, Leu, Ile, Met
, ◉ Describe aliphatic amino acids and their location in proteins. Answer:
Relatively small which allows them to interact with other groups, found
in interior of protein away from water with other aliphatic groups (fold
together)
◉ Why is proline unique?. Answer: its side chain makes a ring by
bonding with its main chain nitrogen
◉ How do non-polar aromatic groups compare to aliphatic? (5 reasons).
Answer: similar to aliphatic in that they are non-polar, but the side
chains of these compounds contain a ring of carbons as an aromatic
functional group, not as small as the aliphatic, but they are more rigid,
aromatic ring structures have unique physical and chemical properties
◉ Why are the benzene rings important in aromatic groups?. Answer:
The double bonds (conjugated system) absorb light well for proteins
◉ Name the 3 non-polar aromatic groups. Answer: Phenylalanine
(Phe,F), Tryptophan (Trp,W), Tyrosine (Tyr,Y)
◉ Describe the polar neutral amino acids and location in proteins.
Answer: side chains that have a dipole, and most can hydrogen bond,
permits these amino acids to interact strongly with water, found on the
outside of the protein and in contact with water
