Free Printable AP Biology: Unit 1 Review

1.

Why does organic chemistry focus on the study of carbon containing compounds?

a)

Carbon is the most abundant element on Earth

b)

Carbon is the easiest element to study

c)

Carbon is backbone of the 4 categories of biomolecules and is found in all living things.

d)

Carbon makes up the largest percentage of living organisms mass

2.

Which elements are found in carbohydrates?

a)

C, H, O

b)

C, H, O, N

c)

C, H, O, P

d)

C, H, O, N, P

3.

Which elements are found in lipids?

a)

C, H, O

b)

C, H, O, N

c)

C, H, O, P

d)

C, H, O, N., P

4.

Which elements are found in proteins?

a)

C, H, O

b)

C, H, O, N

c)

C, H, O, P

d)

C, H, O, N, P

5.

Which elements are found in nucleic acids?

a)

C, H, O

b)

C, H, O, N

c)

C, H, O, P

d)

C, H, O, N, P

6.

What are the structural difference between DNA and RNA?

a)

DNA is double stranded, RNA is single stranded

b)

DNA contains thymine, RNA contains uracil

c)

DNA contains deoxyribose sugar, RNA contains ribose sugar

d)

All of the above

7.

What type of bond holds amino acids together?

a)

Glycosidic bond

b)

Ester bond

c)

Peptide bond

d)

Phosphodiester bond

8.

What type of bonds link monomers in biological polymers?

a)

Ionic bonds

b)

Metallic bonds

c)

Hydrogen bonds

d)

Covalent bonds

9.

In a DNA molecule, what type of bond binds adenine and thymine together?

a)

Peptide bonds

b)

Hydrogen bonds

c)

Covalent bonds

d)

Disulfide bridges

10.

How do monomers combine into polymers?

a)

A molecule of water is added to the monomers forming a new hydrogen bond

b)

A molecule of water is removed between the two monomers, and a covalent bond is formed

c)

They form hydrogen bonds between their polar functional groups.

d)

One monomer takes electrons from the other and they form an ionic bond

11.

How do organisms breakdown polymers into monomers?

a)

By digesting them with powerful enzymes

b)

Through the process of reverse osmosis

c)

By removing water from the polymer, which makes the chain dry and brittle

d)

By adding a molecule of water between the monomers separating them

12.

What is the difference between saturated and unsaturated lipids?

a)

Saturated lipids contain the maximum number of carbon-hydrogen single bonds

b)

Saturated lipids are solids at room temperature

c)

Unsaturated lipids contain double bonds

d)

Unsaturated lipids are easier for our bodies to breakdown

e)

All of the above

13.

What is the strongest type of bond found in a protein?

a)

Peptide bond

b)

Disulfide bridge

c)

Van der Waals interactions

d)

Hydrogen bond

14.

How will altering a protein's primary structure affect its final structure?

a)

An altered primary structure changes every level of structure above it, most likely rendering the protein non-functional

b)

Primary structure does not influence the structure of the protein

c)

The secondary structure will be altered as will but the other levels will remain the same

15.

Why is molecular shape crucial in biology?

a)

The shapes will change based on a cell's needs

b)

Organisms like to look pretty

c)

Structure determines function

d)

The larger the molecule the more biological significance it has

16.

What biomolecules contain nitrogen?

a)

Proteins and Nucleic acids

b)

Carbohydrates and Lipids

c)

Nucleic acids and Carbohydrates

d)

Lipids and Proteins

17.

What is the cause of surface tension in water?

a)

The high density of water

b)

Hydrogen bonds form between the positive hydrogen of one water molecule and the negative oxygen of another

c)

Covalent bonds form between the water molecules

d)

Water's high specific heat

18.

What is cohesion?

a)

Water's ability to form 4 covalent bonds

b)

Water's ability to absorb a large amount of energy

c)

Water's tendency to "stick" to other water molecules

d)

Water's tendency to "stick" to other compounds and surfaces

19.

Where will hydrophobic amino acids orient themselves during protein folding?

a)

At the top of the protein

b)

On the sides of the protein

c)

In the interior of the protein

d)

On the surface of the protein

20.

Where will hydrophilic amino acids orient themselves during protein folding?

a)

They will be found throughout the proteins structure

b)

On the surface of the protein

c)

On the bottom of the protein

d)

In the interior of the protein

21.

What is the primary structure of a protein?

a)

The interaction of multiple polypeptide chains

b)

Folding caused by environmental interactions with the R-groups of the amino acids

c)

The sequence of amino acids

d)

Hydrogen bonds forming between the carbon skeletons of the amino acids

22.

What is the secondary structure of a protein?

a)

The sequence of amino acids

b)

Folding caused by environmental interactions with the R-groups of amino acids

c)

Hydrogen bonds forming between carbon skeletons, creating alpha helixes and beta pleats

d)

Combining of multiple polypeptide chains to form 1 protein

23.

What is the tertiary structure of a protein?

a)

The sequence of amino acids

b)

Folding caused by hydrogen bonds forming between the carbon skeletons

c)

Multiple polypeptides combining to form one protein

d)

Folding caused by environmental interactions with the amino acid R-groups

24.

What is the quaternary structure of a protein?

a)

The sequence of amino acids

b)

When multiple polypeptide chains combine to form one protein

c)

Hydrogen bonds forming between the carbon skeletons of amino acids

d)

Environmental interactions with the R-groups of amino acids

25.

What is the biological significance of water's polarity?

a)

The polarity prevents water from being contaminated with lipids

b)

The polarity allows water to form 4 covalent bonds with its open valence electrons

c)

Being polar allows water to form hydrogen bonds, which give rise to the emergent properties

d)

Water is not polar under most conditions

26.

What structures of an amino acid join to form peptide bonds?

a)

The R-groups of the amino acids bond together

b)

The carboxyl group of one amino acid, with the R group of the next

c)

The carboxyl group of one amino acid, and the amine group of the next

d)

The amine groups join together

27.

What is an enzyme?

a)

A catalyst made of protein

b)

A catalyst made of DNA or RNA

c)

A catalyst made of metals only

28.

Where does a peptide bond form?

a)

between the five-carbon sugar of one nucleotide and the phosphate group of another nucleotide

b)

between the R group of one amino acid and the carboxyl group of another amino acid

c)

between the amino group of one amino acid and the carboxyl group of another amino acid

d)

between the nitrogenous base of one nucleotide and the phosphate group of another nucleotide

29.

Why is carbon able to form a large number of different molecules?

a)

carbon only forms ionic bonds

b)

carbon only forms ring structures

c)

carbon can form four covalent bonds

d)

carbon forms small simple structures

30.

A polar covalent bond between atom occurs when

a)

One of the atoms has a greater affinity for electrons than the other atom

b)

The atoms attract the electrons equally

c)

An electron from one of the atoms is completely transferred to the other atom

d)

The molecule becomes ionized

31.

The basic units or building blocks of fats are

a)

Simple sugars (monosaccharides)

b)

Double sugars (disaccharides)

c)

Amino acids

d)

Glycerol and fatty acids

32.

These molecules are examples of _________.

a)

amino acids

b)

triglycerides

c)

monosaccharides

d)

lipids

33.

The diagram shows the general structure of an amino acid. Which type of molecule is formed from amino acids?

a)

lipids

b)

proteins

c)

carbohydrates

d)

nucleic acids

34.

What is the monomer of a lipid?

a)

Amino Acid

b)

Fatty Acid

c)

Monosaccharides

d)

Glucose

35.

The parts of a nucleotide are:

a)

nitrogen, sulfur, phosphate group

b)

DNA, RNA, ATP

c)

nitrogenous base, ATP, glucose

d)

nitrogenous base, 5-carbon sugar, phosphate group

36.

A ____ reaction releases water molecules while ____ a molecule.

a)

dehydration; building

b)

dehydration; breaking down

c)

hydrolysis; building

d)

hydrolysis; breaking down

37.

A ____ reaction uses a water molecule to ___ a molecule.

a)

dehydration; build

b)

hydrolysis; build

c)

dehydration; break down

d)

hydrolysis; break down

38.

The linkages formed between nucleotides are called ___ bonds.

a)

peptide

b)

ester

c)

phosphodiester

d)

glycosidic

39.

To which class of macromolecules does this molecule belong?

a)

carbohydrates

b)

lipids

c)

proteins

d)

nucleic acids

40.

To which class of macromolecules does this hormone molecule belong?

a)

carbohydrates

b)

lipids

c)

proteins

d)

nucleic acids

41.

To which class of macromolecules does this molecule belong?

a)

carbohydrates

b)

lipids

c)

proteins

d)

nucleic acids

42.

To which class of macromolecules does this molecule belong?

a)

carbohydrates

b)

lipids

c)

proteins

d)

nucleic acids

43.

To which class of macromolecules does this molecule belong?

a)

carbohydrates

b)

lipids

c)

proteins

d)

nucleic acids

44.

Which type of carbohydrate is this?

a)

monsaccharide

b)

disaccharide

c)

polysaccharide

d)

glyceride

45.

What functional group is shown in red?

a)

carboxyl group

b)

hydroxyl group

c)

amino group

d)

phosphate group

46.

What functional group is shown in red?

a)

carboxyl group

b)

hydroxyl group

c)

amino group

d)

phosphate group

47.

Which functional group is shown in red?

a)

carboxyl group

b)

hydroxyl group

c)

amino group

d)

phosphate group

48.

Which functional group is shown?

a)

carboxyl group

b)

hydroxyl group

c)

amino group

d)

phosphate group

49.

What functional group is shown in yellow?

a)

amino group

b)

phosphate group

c)

carbonyl group

d)

sulfhydryl group

50.

Which functional group makes di-sulfide bridges in protein formation?

a)

amino group

b)

phosphate group

c)

carbonyl group

d)

sulfhydryl group

51.

Alcohols have this functional group:

a)

carboxyl group

b)

hydroxyl group

c)

amino group

d)

phosphate group

52.

Proteins contain this functional group:

a)

carboxyl group

b)

hydroxyl group

c)

amino group

d)

phosphate group

53.

This molecule is...

a)

A saturated fatty acid

b)

An unsaturated fatty acid

c)

Glycerol

d)

Glucose

54.

This molecule is...

a)

A saturated fatty acid

b)

An unsaturated fatty acid

c)

Glycerol

d)

Glucose

55.

In a normal cellular protein, where would you expect to find a hydrophobic amino acid such as valine?

a)

in the interior of the folded protein, away from water

b)

on the exterior surface of the protein, interacting with water

c)

in the transmembrane portion interacting with lipid fatty acid chains

d)

in the interior of the folded protein, away from water, or in a transmembrane portion interacting with lipid fatty acid chains

56.

There are 20 different amino acids. What makes one amino acid different from another?

a)

different side chains (R groups) attached to a carboxyl carbon

b)

different side chains (R groups) attached to the amino groups

c)

different side chains (R groups) attached to an α carbon

d)

different structural and optical isomers

57.

Polysaccharides, triacyl-glycerides, and proteins are similar in that they

a)

are synthesized from monomers by the process of hydrolysis.

b)

are synthesized from subunits by dehydration reactions.

c)

are synthesized as a result of peptide bond formation between monomers.

d)

are decomposed into their subunits by dehydration reactions.

58.

A carbon skeleton is covalently bonded to both an amino group and a carboxyl group. When placed in water it

a)

would function only as an acid because of the carboxyl group.

b)

would function only as a base because of the amino group.

c)

would function as neither an acid nor a base.

d)

would function as both an acid and a base.

59.

Which two functional groups are always found in amino acids?

a)

ketone and methyl

b)

carbonyl and amino

c)

carboxyl and amino

d)

amino and sulfhydryl

60.

What is the difference between covalent bonds and ionic bonds?

a)

Covalent bonds are formed between atoms to form molecules; ionic bonds are formed between atoms to form compounds.

b)

Covalent bonds involve the sharing of pairs of electrons between atoms; ionic bonds involve the sharing of single electrons between atoms.

c)

Covalent bonds involve the sharing of electrons between atoms; ionic bonds involve the electrical attraction between atoms.

d)

Covalent bonds involve the sharing of electrons between atoms; ionic bonds involve the sharing of protons between atoms.

61.

Which bond or interaction would be difficult to disrupt when compounds are put into water? Think about the polarity of water as it acts as a solvent.

a)

covalent bond

b)

hydrogen bond

c)

van der Waals interaction

d)

ionic bond

62.

Which explanation best describes how a PEPTIDE BOND determines a protein's structure?

a)

A chemical bond formed between two ions of opposite charges. In a protein, bonds form between the ionized acidic or basic groups of amino acids. This bond can be broken if the pH level changes and can cause the denaturation of proteins. This bond stabilized Tertiary and Quaternary structures.

b)

Forms amino acid chains (primary structure) due to a covalent bond formed between a carboxyl group of an amino acid and the R-group of another amino acid to create a polypeptide.

c)

Covalent bonds between sulfurs in sulfhydryl (-SH) side groups that reinforce the tertiary structures of a protein.

d)

Bonds present in the-OH group of –NH2 of amino acids become slightly electropositive. Bonds between the oxygen (δ-) atoms and hydrogen (δ+) atoms attached to the nitrogen help stabilize the polypeptide backbone. Results in an 𝛂 Helix or 𝛃 Pleated Sheet. High frequency of these bonds leads to high stability of proteins at the secondary, tertiary, and quaternary levels.

63.

Which explanation best describes how an IONIC BOND determines a protein's structure?

a)

A chemical bond formed between two ions of opposite charges. In a protein, bonds form between the ionized acidic or basic groups of amino acids. This bond can be broken if the pH level changes and can cause the denaturation of proteins. This bond stabilized Tertiary and Quaternary structures.

b)

Forms amino acid chains (primary structure) due to a covalent bond formed between a carboxyl group of an amino acid and the R-group of another amino acid to create a polypeptide.

c)

Covalent bonds between sulfurs in sulfhydryl (-SH) side groups that reinforce the tertiary structures of a protein.

d)

Bonds present in the-OH group of –NH2 of amino acids become slightly electropositive. Bonds between the oxygen (δ-) atoms and hydrogen (δ+) atoms attached to the nitrogen help stabilize the polypeptide backbone. Results in an 𝛂 Helix or 𝛃 Pleated Sheet. High frequency of these bonds leads to high stability of proteins at the secondary, tertiary, and quaternary levels.

64.

Which explanation best describes how a DISULFIDE BRIDGE determines a protein's structure?

a)

A chemical bond formed between two ions of opposite charges. In a protein, bonds form between the ionized acidic or basic groups of amino acids. This bond can be broken if the pH level changes and can cause the denaturation of proteins. This bond stabilized Tertiary and Quaternary structures.

b)

Forms amino acid chains (primary structure) due to a covalent bond formed between a carboxyl group of an amino acid and the R-group of another amino acid to create a polypeptide.

c)

Covalent bonds between sulfurs in sulfhydryl (-SH) side groups that reinforce the tertiary structures of a protein.

d)

Bonds present in the-OH group of –NH2 of amino acids become slightly electropositive. Bonds between the oxygen (δ-) atoms and hydrogen (δ+) atoms attached to the nitrogen help stabilize the polypeptide backbone. Results in an 𝛂 Helix or 𝛃 Pleated Sheet. High frequency of these bonds leads to high stability of proteins at the secondary, tertiary, and quaternary levels.

65.

Which explanation best describes how a HYDROGEN BOND determines a protein's structure?

a)

A chemical bond formed between two ions of opposite charges. In a protein, bonds form between the ionized acidic or basic groups of amino acids. This bond can be broken if the pH level changes and can cause the denaturation of proteins. This bond stabilized Tertiary and Quaternary structures.

b)

Forms amino acid chains (primary structure) due to a covalent bond formed between a carboxyl group of an amino acid and the R-group of another amino acid to create a polypeptide.

c)

Covalent bonds between sulfurs in sulfhydryl (-SH) side groups that reinforce the tertiary structures of a protein.

d)

Bonds present in the-OH group of –NH2 of amino acids become slightly electropositive. Bonds between the oxygen (δ-) atoms and hydrogen (δ+) atoms attached to the nitrogen help stabilize the polypeptide backbone. Results in an 𝛂 Helix or 𝛃 Pleated Sheet. High frequency of these bonds leads to high stability of proteins at the secondary, tertiary, and quaternary levels.

66.

Which explanation best describes how a HYDROPHOBIC INTERACTION determines a protein's structure?

a)

A chemical bond formed between two ions of opposite charges. In a protein, bonds form between the ionized acidic or basic groups of amino acids. This bond can be broken if the pH level changes and can cause the denaturation of proteins. This bond stabilized Tertiary and Quaternary structures.

b)

Forms amino acid chains (primary structure) due to a covalent bond formed between a carboxyl group of an amino acid and the R-group of another amino acid to create a polypeptide.

c)

Due to some R-Groups in amino acids being non-polar, when these polypeptide chains are in an aqueous environment, such as a cell, the polypeptide will fold into a shape that has the non-polar amino acids come into close contact with each other. This results in a globular protein shape.

d)

Bonds present in the-OH group of –NH2 of amino acids become slightly electropositive. Bonds between the oxygen (δ-) atoms and hydrogen (δ+) atoms attached to the nitrogen help stabilize the polypeptide backbone. Results in an 𝛂 Helix or 𝛃 Pleated Sheet. High frequency of these bonds leads to high stability of proteins at the secondary, tertiary, and quaternary levels.

AP Biology: Unit 1 Review

Total questions: 66

Worksheet time: 17hrs 30mins

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