1.2&1.3&1.4 Ms

AP Biology Scoring Guide
1.2&1.3&1.4
1. Which of the following best describes how amino acids affect the tertiary structure of a protein?
A The number of amino acids determines the tertiary structure of the protein.
The interactions of the different -groups with other -groups and with their environment determine the
B
tertiary structure of the protein.
The -group of the last amino acid that is added to a growing polypeptide chain determines the next amino
C
acid that is added to the chain.
The sequence of the amino acids in the polypeptide chain determines the protein’s primary structure but has
D
no effect on its tertiary structure.
2. Which of the following correctly illustrates a dipeptide and an amino acid in the optimal position to form a
tripeptide?
Copyright © 2021. The College Board. These materials are part of a College Board program. Use or distribution of these materials online or in print
beyond your school’s participation in the program is prohibited.
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3. The molecular structures of linoleic acid and palmitic acid, two naturally occurring substances, are shown in
the figure.
Based on the molecular structures shown in the figure, which molecule is likely to be solid at room
temperature?
Linoleic acid, because the absence of carbon-carbon double bonds allows the molecules to pack closely
A
together.
Linoleic acid, because the presence of carbon-carbon double bonds prevents the molecules from packing
B
closely together.
Palmitic acid, because the absence of carbon-carbon double bonds allows the molecules to pack closely
C
together.
Palmitic acid, because the presence of carbon-carbon double bonds prevents the molecules from packing
D
closely together.
Directions: This group of questions consists of five lettered headings followed by a list of phrases or sentences.
For each phrase or sentence, select the one heading to which it is most closely related. Each heading may be used
once, more than once, or not at all.
This group of questions refers to the following groups of biological compounds.
(A) Proteins
(B) Carbohydrates
(C) Nucleic acids
(D) Lipids
(E) Steroids
4. Used to carry the genetic code
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A Proteins
B Carbohydrates
C Nucleic acids
D Lipids
E Steroids
5. Which of the following best describes the hydrolysis of carbohydrates?
A The removal of a water molecule breaks a covalent bond between sugar monomers.
B The removal of a water molecule forms a covalent bond between sugar monomers.
C The addition of a water molecule breaks a covalent bond between sugar monomers.
D The addition of a water molecule forms a covalent bond between sugar monomers.
6. A feature of organic compounds NOT found in inorganic compounds is the presence of
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A ionizing chemical groups
B electrons
C carbon atoms covalently bonded to each other
D oxygen
E hydrogen bonds
7. Which of the following best explains why a cell’s plasma membrane is composed of two layers of
phospholipids rather than just a single layer?
Having two oppositely oriented layers of phospholipids allows only the hydrophilic heads to interact with
A
water inside and outside of the cell.
Having two oppositely oriented layers of phospholipids allows the hydrophilic heads to repel water both
B
inside and outside of the cells.
Having two identically oriented layers of phospholipids gives cells more protection from the exterior
C
environment than just a single layer would.
Having two identically oriented layers of phospholipids allows for the production of vacuoles while still
D
maintaining a protective barrier.
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8. Figure 1 represents a common process that occurs in organisms.
Figure 1. Structural formula for a common biological reaction

Which of the following is an accurate description of the process shown in Figure 1 ?
A The linking of amino acids with an ionic bond as an initial step in the protein synthesis process
B The formation of a more complex carbohydrate with the covalent bonding of two simple sugars
C The hydrolysis of amino acids with the breaking of covalent bonds with the release of water
D The formation of a covalent peptide bond in a dehydration synthesis reaction
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9.
Figure 1. Formation of a peptide bond

Which of the following best describes the formation of the bond shown in Figure 1 ?
An ionic bond is formed between a carbon atom of one amino acid and the nitrogen atom of the other amino
A
acid.
An ionic bond is formed when the negative charge of an group is balanced by the positive charge of a
B
hydrogen ion.
C A covalent bond is formed between a carbon atom and a nitrogen atom along with the formation of .
D A covalent bond is formed that replaces the hydrogen bond between the group and the atom.
10. Which of the following best describes the structures of carbohydrates?
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A They only occur as disaccharides.
B They occur as monomers, chains of monomers, and branched structures.
C They only occur as long and branched structures.
D They occur as chains of monomers that hydrogen bond with complementary chains of monomers.
11. The synthesis of protein or carbohydrate polymers always produces which of the following as a byproduct?
A ATP
B Oxygen
C Carbon dioxide
D Urea
E Water
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12. Polypeptides are continuously being formed and degraded. One of these processes is shown.
Figure 1. Polypeptide reaction

Which statement is the most accurate description of the reaction shown in Figure 1?
A It represents monomers linked by dehydration synthesis.
B It represents a polypeptide chain that folds to form the tertiary structure.
C It represents a polypeptide chain that is denatured into the primary structure.
D It represents a polypeptide chain that is broken down through a hydrolysis reaction.
13. Directions: This short free-response question requires about 6 minutes to answer. The question is worth
3 points. Read the question carefully and completely. Answers must be written out in paragraph form.
Outlines, bulleted lists, or diagrams alone are not acceptable.
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The graph above shows the initial rate of an enzyme-catalyzed reaction at different substrate
concentrations in the presence of a constant concentration of the enzyme.
(a) Connect the primary structure of the enzyme to its overall shape.
Please respond on separate paper, following directions from your teacher.
(b) Predict the effect of adding a noncompetitive inhibitor to the reaction mixture on the rate of
reaction at a high substrate concentration. Support your prediction by describing how a noncompetitive
inhibitor affects the structure and function of an enzyme.
Part A
1 point maximum
Connection (1 point)
· The amino acid sequence determines the overall shape (of the polypeptide/protein/enzyme)
· R- groups interact and stabilize the structure
0 1
Student response earns one of the following points.
Connection (1 point)
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· The amino acid sequence determines the overall shape (of the polypeptide/protein/enzyme)
· R- groups interact and stabilize the structure
Part B
2 points maximum
Prediction (1 point)
· Noncompetitive/allosteric inhibitor will decrease the (initial) rate of reaction (at any substrate concentration)
Support (1 point)
· Inhibitor binding to site other than active site (allosteric site) changes shape of enzyme, which alters the
interaction of substrate with active site
0 1 2
Student response earns two of the following points.
Prediction (1 point)
· Noncompetitive/allosteric inhibitor will decrease the (initial) rate of reaction (at any substrate concentration)
Support (1 point)
· Inhibitor binding to site other than active site (allosteric site) changes shape of enzyme, which alters the
interaction of substrate with active site
14. Directions: Answers must be in essay form. Outline form is not acceptable. Labeled diagrams may be
used to supplement discussion, but in no case will a diagram alone suffice. It is important that you read
each question completely before you begin.
Proteins–large complex molecules–are major building blocks of all living organisms. Discuss the
following in relation to proteins.
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(a) The chemical composition and levels of structure of proteins
(b) The roles of DNA and RNA in protein synthesis
(c) The roles of proteins in membrane structure and transport of molecules across the membrane
Part A
4 points maximum
Chemical composition — 2 points maximum
1 point amino acids are the basic building blocks of proteins
1 point amino acids contain amino, carboxyl and R groups
or
correct structural formula showing amino, carboxyl, and R group attached to central carbon
or
proteins are composed of carbon, hydrogen, oxygen and nitrogen
1 point R group determines the identity/properties of the amino acid
Elaboration
1 point for a description of addition of lipids, carbohydrates, and/or prosthetic group
Levels of structure — 3 points maximum (Note: to obtain any points, response must name level or list in correct
order.)
Primary structure — 1 point
· sequence (chain, string) of amino acids or the number and order of amino acids
· amino acids linked by peptide bonds
· amino acids bonded through dehydration synthesis
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Secondary structure — 1 point
· helix and/or pleated sheet
· hydrogen bonds (between carboxyl and amino groups)
Tertiary structure — 1 point
· single polypeptide chain forms globular shape
· hydrogen, ionic, disulfide, and van der Waals bonds, and/or hydrophobic interactions (if hydrogen must have
more than one)
· interaction between R groups
Quaternary structure — 1 point
· more than one polypeptide or subunit
more than one)
Elaboration — 1 point
· explanation of domains
· explanation of chaperones
0 1 2 3 4
Student response earns four of the available points.
Chemical composition — 2 points maximum
or
correct structural formula showing amino, carboxyl, and R group attached to central carbon
or
proteins are composed of carbon, hydrogen, oxygen and nitrogen
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Elaboration
Levels of structure — 3 points maximum (Note: to obtain any points, response must name level or list in correct
order.)
Primary structure — 1 point
· sequence (chain, string) of amino acids or the number and order of amino acids
· amino acids linked by peptide bonds
· amino acids bonded through dehydration synthesis
Secondary structure — 1 point
· helix and/or pleated sheet
· hydrogen bonds (between carboxyl and amino groups)
Tertiary structure — 1 point
· single polypeptide chain forms globular shape
more than one)
Quaternary structure — 1 point
· more than one polypeptide or subunit
more than one)
· explanation of domains
· explanation of chaperones
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Part B
4 points maximum
Global understanding of information flow — 1 point
· information in DNA is transcribed to mRNA which is translated into protein
· DNA contains the information that ultimately determines the sequence of amino acids in the protein
Roles
DNA — 1 point
· codes for RNA, mRNA, tRNA, or rRNA
mRNA — 1 point
· codes for amino acid sequence
tRNA — 1 point
· brings the correct amino acid to the ribosome/mRNA
· contains anticodon complementary to codon
rRNA — 1 point
· forms part of ribosome
· intron removal by RNA/snRNP/snRNA
· alternative splicing provides protein diversity
· acts as ribozyme/involved in formation of peptide bond
· rRNA finds and binds start AUG of mRNA (in prokaryotes)
0 1 2 3 4

Global understanding of information flow — 1 point
· information in DNA is transcribed to mRNA which is translated into protein
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· DNA contains the information that ultimately determines the sequence of amino acids in the protein
Roles
DNA — 1 point
· codes for RNA, mRNA, tRNA, or rRNA
mRNA — 1 point
· codes for amino acid sequence
tRNA — 1 point
· brings the correct amino acid to the ribosome/mRNA
· contains anticodon complementary to codon
rRNA — 1 point
· forms part of ribosome
· intron removal by RNA/snRNP/snRNA
· alternative splicing provides protein diversity
· acts as ribozyme/involved in formation of peptide bond
· rRNA finds and binds start AUG of mRNA (in prokaryotes)
Part C
4 points maximum
Role in membrane structure — 2 points maximum
1 point — description of integral and/or peripheral proteins
1 point — membrane synthesis
1 point — defines membrane sidedness
Membrane function other than transport
1 point — receptors
1 point — enzymes
1 point — cell to cell communication
1 point — anchoring of cytoskeleton or extracellular matrix
1 point — spatial configuration of reaction pathways (e.g., electron transport system)
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1 point — cell recognition

1 point — cell junctions
Role in transport — 3 points maximum

1 point — transport proteins may be specific
1 point — process may require direct input of energy (e.g., use of ATP)
1 point — description of transport mechanisms (bind molecule, conformational change, release molecule) or
description of how proteins form channels and move molecules through them
· description of a specific transport system (e.g., ATP synthase, pump, receptor mediated endocytosis)
· description of chemiosmosis
· more than one molecule transported (e.g., symport, antiport)
· may be regulated by electrical or chemical stimuli (gated channels)
0 1 2 3 4
Role in membrane structure — 2 points maximum

1 point — description of integral and/or peripheral proteins
1 point — membrane synthesis
1 point — defines membrane sidedness
Membrane function other than transport
1 point — receptors
1 point — enzymes
1 point — cell to cell communication
1 point — anchoring of cytoskeleton or extracellular matrix
1 point — spatial configuration of reaction pathways (e.g., electron transport system)
1 point — cell recognition
1 point — cell junctions
Role in transport — 3 points maximum

1 point — transport proteins may be specific
1 point — process may require direct input of energy (e.g., use of ATP)
1 point — description of transport mechanisms (bind molecule, conformational change, release molecule) or
description of how proteins form channels and move molecules through them
· description of a specific transport system (e.g., ATP synthase, pump, receptor mediated endocytosis)
· description of chemiosmosis
· more than one molecule transported (e.g., symport, antiport)
· may be regulated by electrical or chemical stimuli (gated channels)
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Directions: Answers must be in essay form. Outline form is not acceptable. Labeled diagrams may be used to
supplement discussion, but in no case will a diagram alone suffice. It is important that you read each question
completely before you begin.
Proteins–large complex molecules–are major building blocks of all living organisms. Discuss the following in
relation to proteins.
15. The chemical composition and levels of structure of proteins
General
4 points maximum
Chemical composition - 2 points maximum

ORcorrect structural formula showing amino, carboxyl, and R group attached to central carbon
OR proteins are composed of carbon, hydrogen, oxygen and nitrogen
Elaboration
Levels of structure - 3 points maximum (Note: to obtain any points, response must name level or list in
correct order.)
Primary structure - 1 point
sequence (chain, string) of amino acids or the number and order of amino acids
amino acids linked by peptide bonds
amino acids bonded through dehydration synthesis
Secondary structure - 1 point
helix and/or pleated sheet

hydrogen bonds (between carboxyl and amino groups)
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Tertiary structure - 1 point
single polypeptide chain forms globular shape

hydrogen, ionic, disulfide, and van der Waals bonds, and/or hydrophobic interactions (if hydrogen musthave
more than one)
interaction between R groups
Quaternary structure - 1 point
more than one polypeptide or subunit

more than one)
Elaboration - 1 point
explanation of domains
explanation of chaperones
0 1 2 3 4
4 points maximum
Chemical composition - 2 points maximum

ORcorrect structural formula showing amino, carboxyl, and R group attached to central carbon
OR proteins are composed of carbon, hydrogen, oxygen and nitrogen
Elaboration
Levels of structure - 3 points maximum (Note: to obtain any points, response must name level or list in
correct order.)
Primary structure - 1 point
sequence (chain, string) of amino acids or the number and order of amino acids
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amino acids linked by peptide bonds

amino acids bonded through dehydration synthesis
Secondary structure - 1 point
helix and/or pleated sheet

hydrogen bonds (between carboxyl and amino groups)
Tertiary structure - 1 point
single polypeptide chain forms globular shape

more than one)
Quaternary structure - 1 point
more than one polypeptide or subunit

more than one)
Elaboration - 1 point
explanation of domains
explanation of chaperones
Copyright © 2021. The College Board. These materials are part of a College Board program. Use or distribution of these materials online or in print beyond your school’s
participation in the program is prohibited.
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AP Biology Scoring Guide

This group of questions refers to the following groups of biological compounds.

4. Used to carry the genetic code

5. Which of the following best describes the hydrolysis of carbohydrates?

6. A feature of organic compounds NOT found in inorganic compounds is the presence of

A ionizing chemical groups

C carbon atoms covalently bonded to each other

8. Figure 1 represents a common process that occurs in organisms.

Figure 1. Structural formula for a common biological reaction

D The formation of a covalent peptide bond in a dehydration synthesis reaction

Figure 1. Formation of a peptide bond

10. Which of the following best describes the structures of carbohydrates?

A They only occur as disaccharides.

B They occur as monomers, chains of monomers, and branched structures.

C They only occur as long and branched structures.

Figure 1. Polypeptide reaction

A It represents monomers linked by dehydration synthesis.

B It represents a polypeptide chain that folds to form the tertiary structure.

C It represents a polypeptide chain that is denatured into the primary structure.

D It represents a polypeptide chain that is broken down through a hydrolysis reaction.

Please respond on separate paper, following directions from your teacher.

Please respond on separate paper, following directions from your teacher.

· R- groups interact and stabilize the structure

Student response earns one of the following points.

· R- groups interact and stabilize the structure

Student response earns two of the following points.

(a) The chemical composition and levels of structure of proteins

Please respond on separate paper, following directions from your teacher.

(b) The roles of DNA and RNA in protein synthesis

Please respond on separate paper, following directions from your teacher.

Please respond on separate paper, following directions from your teacher.

1 point amino acids are the basic building blocks of proteins

1 point amino acids contain amino, carboxyl and R groups

1 point R group determines the identity/properties of the amino acid

1 point for a description of addition of lipids, carbohydrates, and/or prosthetic group

Primary structure — 1 point

· amino acids linked by peptide bonds

· amino acids bonded through dehydration synthesis

Secondary structure — 1 point

· helix and/or pleated sheet

· hydrogen bonds (between carboxyl and amino groups)

Tertiary structure — 1 point

· single polypeptide chain forms globular shape

· interaction between R groups

Quaternary structure — 1 point

· more than one polypeptide or subunit

· interaction between R groups

Student response earns four of the available points.

Chemical composition — 2 points maximum

1 point amino acids are the basic building blocks of proteins

1 point amino acids contain amino, carboxyl and R groups

1 point R group determines the identity/properties of the amino acid

1 point for a description of addition of lipids, carbohydrates, and/or prosthetic group

Primary structure — 1 point

· amino acids linked by peptide bonds

· amino acids bonded through dehydration synthesis

Secondary structure — 1 point

· helix and/or pleated sheet

· hydrogen bonds (between carboxyl and amino groups)

Tertiary structure — 1 point

· single polypeptide chain forms globular shape

· interaction between R groups

Quaternary structure — 1 point