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(Unit 1) Chapter 5: The Structure and Function of Large Biological Molecules Flashcards

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1
Q

The critically important large molecules of all living things fall into just ___ main classes:

A

Four

Carbohydrates, lipids, proteins, and nucleic acids

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2
Q

What are called macromolecules? Why?

A

Carbohydrates, proteins, nucleic acids

On molecular scale, they are huge (e.x. 1 protein may have a mass of well over 100,000 daltons)

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3
Q

Define:

Polymer

A

A long molecule consisting of many similar or identical building blocks linked by covalent bonds

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4
Q

Define:

Monomers

A

The smaller molecules and repeating units that serve as the building blocks of a polymer

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5
Q

How are monomers connected?

A

Through condensation reaction, specifically a dehydration reaction

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6
Q

How does a dehydration reaction work?

A

A type of condensation reaction where two molecules are covalently bonded to each other through loss of a water molecule (thus dehydration)

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7
Q

Define:

Enzymes

A

Specialized macromolecules that speed up chemical reactions in cells

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8
Q

How are polymers disassembled to monomers?

A

Hydrolysis

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9
Q

Define:

Hydrolysis

A

A process that is essentially the reverse of dehydration reaction, thus bonds are broken b the addition of water

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10
Q

Where does the word polymer come from?

A

Greek polys (many) and meris (part)

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11
Q

Where does the word hydrolysis come from?

A

Greek hydro (water) and lysis (break)

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12
Q

Carbohydrates include both ______ and ________ of ______

A

Sugar
Polymers
Sugars

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13
Q

What are simple sugars known as?

A

Monosaccharides

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14
Q

What are disaccharides?

A

Double sugars, consisting of two monosaccharides joined by a covalent bond

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15
Q

Define:

Polysaccharides

A

Polymers composed of many sugar building blocks

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16
Q

Where does the word monosaccharides come from?

A

Greek mono (single) and sacchar (sugar)

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17
Q

What is general formula for a monosaccharide?

A

Some multiple of the unit CH2O

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18
Q

List the sources of diversity for simple sugars (3)

A

The location of the carbonyl group (ketoses or aldoses)
The size of the carbon skeleton
The spatial arrangement of their parts around asymmetric carbons

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19
Q

Define:

Asymmetric carbon

A

A carbon attached to four different atoms or groups of atoms

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20
Q

For sugars, how long do the carbon skeleton range from? What are they called?

A

3 to 7 carbons

Trioses (3-carbon), pentoses (5-carbon), hexoses (6-carbon)

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21
Q

Glyceraldehyde and Dihydroxyacetone are:

A

Trioses, glyceraldehyde is an aldose while dihydroxyacetone is a ketone

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22
Q

Ribose and Ribulose are:

A

Pentoses, ribose is an aldose while ribulose is a ketone

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23
Q

Glucose and Fructose are:

A

Hexoses, glucose is an aldose while fructose is a ketone

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24
Q

What is the difference between glucose and galactose?

A

Only differ in the placement of parts (hydroxyl group and hydrogen) around asymmetric carbons

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25
Q

Monosaccharides are major _________ for cells; How do cells extract energy from glucose?

A

Nutrients

Through cellular respiration

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26
Q

Define:

Disaccharide

A

Consists of two monosaccharides joined by a glycosidic linkage

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27
Q

Define:

Glycosidic linkage

A

A covalent bond formed between two monosaccharides by a dehydration reaction

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28
Q

What are examples of disaccharides? (List the monosaccharides in their formation in brackets) (3)

A

Maltose (glucose and glucose), sucrose (glucose and fructose), lactose (glucose and galactose)

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29
Q

Where is maltose present?
Where is sucrose present?
Where is lactose present?

A

Known as malt sugar, used in brewing beer
Known as table sugar
Present in milk

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30
Q

In aqueous solutions, glucose molecules, as well as most other sugars form what?

A

Rings

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31
Q

In abbreviated ring structure, what do the corners of the ring represent?

A

Carbons

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32
Q

Define:

Polysaccharide

A

A macromolecule, polymers with a few hundred to a few thousand monosaccharides joined by glycosidic linkages

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33
Q

What type of linkage is between the two glucose molecules in maltose?

A

1-4 glycosidic linkage

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34
Q

What type of linkage is between the glucose and fructose molecules in sucrose?

A

1-2 glycosidic linkage

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35
Q

Even though fructose is a hexose, it forms a ____-sided ring

A

Five

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36
Q

Plants and animals store ______ for later use in the form of:

A

Sugars

Storage polysaccharides

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37
Q

What storage polysaccharides do plants use?

A

Starch, a polymer of glucose monomers

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38
Q

Where do plants store starch?

A

As granules within cellular structures known as plastids, which include chloroplasts

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39
Q

How are glucose monomers in starch joined?

A

1-4 glycosidic linkage

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40
Q

What storage polysaccharides do animals use?

A

Glycogen, a polymer of glucose that is like amylopectin but more extensively branched

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41
Q

Where do humans and other vertebrates store glycogen?

A

Mainly in liver and muscle cells

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42
Q

True or False:

Glycogen stores are depleted in about a day

A

True, unless they are replenished by consumption of food

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43
Q

Organisms build strong materials from:

A

Structural polysaccharides

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44
Q

The polysaccharide _________ is a major component of the tough walls that enclose plant cells. On a global scale, plants produce almost __^__ kg (___ _______ tons) per year

A

Cellulose
10^14
100 billion

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45
Q

What is the difference between starch and cellulose? (2)

A

In starch, glucose monomers are in alpha formation (they are in beta formation in cellulose)
Starch molecule is mostly helical while cellulose molecules are straight

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46
Q

What is the difference between alpha and beta glucose?

A

In alpha glucose, the hydroxyl group on carbon 1 is positioned below the plane of the ring
In beta glucose, the hydroxyl group on carbon 1 is positioned above the plane of the ring

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47
Q

True or False:

Cellulose is sometimes branched

A

False, cellulose is never branched

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48
Q

The hydrogen bonding between some hydroxyl groups of cellulose, parallel cellulose molecules held together this way are grouped into units called:

A

Microfibrils

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49
Q

Enzymes that digest starch by ___________its alpha linkages are unable to hydrolyze the beta linkages of _________ because of the distinctly different shapes of these two molecules

A

Hydrolyzing

Cellulose

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50
Q

On food packages, what does “insoluble fiber” mainly refer to?

A

Cellulose

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51
Q

Some ___________ can digest cellulose

A

Prokaryotes

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52
Q

Cows harbour cellulose-digesting prokaryotes in its _____, the first compartment in its _______

A

Rumen

Stomach

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53
Q

Define:

Chitin

A

The carbohydrate used by arthropods (insects, spiders, crustaceans, and related animals) to build their exoskeleton)

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54
Q

Define:

Exoskeleton

A

A hard case the surrounds the soft parts of an animal

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55
Q

True of False:

Pure chitin is hard

A

False, pure chitin is leathery but becomes hardened when encrusted with calcium carbonate (a salt)

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56
Q

True or False:

Chitin is found in fungi, who use it instead of cellulose

A

True

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57
Q

Describe the structure of chitin monomer

A

Similar to glucose monomer of cellulose except that it also has nitrogen containing appendage

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58
Q

Compounds called Lipids are group together due to one important trait:

A

They mix poorly, if at all, with water

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59
Q

What is fat constructed from?

A

Two kinds of smaller molecules: glycerol and fatty acids

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60
Q

Define:

Glycerol

A

An alcohol with three carbons, each bearing a hydroxyl group

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61
Q

Describe the structure of a fatty acid

A

Has a long carbon skeleton, usually 16 or 18 in length

The carbon at one end of the chain is part of a carboxyl group

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62
Q

In making a fat, ______ fatty acid molecules each join to glycerol by an ____________. The resulting fat is called a _______________

A

Three
Ester linkage
Triacylglycerol

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63
Q

Define:

Ester linkage

A

A bond between a hydroxyl group and a carboxyl group

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64
Q

What is a triacylglycerol also called?

A

Triglyceride

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65
Q

True or False:

Fatty acids vary in length and in the number and locations of double bonds

A

True

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66
Q

If there are no double bonds between carbon atoms in the chain of a fatty acid, what is it known as?

A

Saturated fatty acid (as it is saturated with hydrogen)

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67
Q

If there is one or more double bonds in the chain of a fatty acid, what is it known as?

A

Unsaturated fatty acid

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68
Q

The fatty acid will have a kink in the chain wherever:

A

There is a cis double bond

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69
Q

Fat made from saturated fatty acids is called:

A

Saturated fat

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70
Q

The lack of double bonds in saturated fats and flexibility allow the fat molecules to pack tightly in an _________ ___,

A

Saturated fat

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71
Q

Saturated animal fats are _____ at room temperature

A

Solid

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72
Q

Why are unsaturated fats (e.x. fish and plant fats) liquid at room temperature?

A

The kinks due to cis double bonds prevent molecules from packing together closely

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73
Q

Hydrogenating unsaturated fats can also produce fats with _____ double bonds

A

Trans

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74
Q

True or False:
Diet rich in saturated fats is one of several factors that may contribute to cardiovascular disease known as atherosclerosis

A

True

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75
Q

Why are fats useful? (3)

A

Fats can store more than twice as much energy as starch
Can cushion vital organs such as kidneys
Can also insulate the body

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76
Q

Describe the structure of a phospholipid (3)

A

Only two fatty acids attached to glycerol
The third hydroxyl group of glycerol is joined to a phosphate group (has negative charge)
Additional small molecules (usually charged or polar) can be linked to the phosphate group to form a variety of phospholipids

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77
Q

True of False:

The two ends of phospholipids are both hydrophobic

A

False, hydrocarbon tails are hydrophobic while phosphate group and attachments form a hydrophilic head

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78
Q

When phospholipids are added to water, what happens?

A

They assemble into a bilayer that shield the hydrophobic sections away from water

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79
Q

True or False:

At the surface of the cell, phospholipids are arranged in a similar bilayer

A

True

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80
Q

Is it true that cells could not exist without phospholipids?

A

True

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81
Q

Define:

Steroid

A

Lipids that are characterized by a carbon skeleton consisting of four fused rings

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82
Q

What is cholesterol?

A

A common component of animal cell membranes, also the precursor from which other steroids are synthesized in vertebrates

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83
Q

Where is cholesterol synthesized in vertebrates?

A

In the liver

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84
Q

Where does the word protein come from?

A

Greek proteios (first place)

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85
Q

Name the types of proteins (8)

A 
Enzymatic proteins
Structural proteins
Storage proteins
Transport proteins
Hormonal proteins
Receptor proteins
Contractile and motor proteins
Defensive proteins
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86
Q

State the function and example of:

Enzymatic proteins

A 
Selective acceleration of chemical reactions
Digestive enzymes (catalyse hydrolysis of polymers in food)
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87
Q

State the function and example (3) of:

Structural proteins

A

Support
Collagen and elastin provide fibrous framework in animal connective tissues
Keratin is protein of hair, horns, feathers and other skin appendages

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88
Q

State the function and example (2) of:

Storage proteins

A

Storage of amino acids
Ovalalbumin is the protein of egg white (used as amino acid source for developing embryos)
Casein, protein in milk, is major source of amino acids for baby mammals

89
Q

State the function and example of:

Transport proteins

A

Transport of other substances

Hemoglobin transports oxygen from lungs to other parts of other body

90
Q

State the function and example of:

Hormonal proteins

A

Coordination of an organism’s activities

Insulin (hormone secreted by pancreas) helps regulate the concentration of sugar in the blood of vertebrates

91
Q

State the function and example (2) of:

Contractile and motor proteins

A

Movement

Actin and myosin are responsible for contraction of muscles

92
Q

State the function and example of:

Receptor proteins

A

Response of cell to chemical stimuli

Receptors built into nerve cells detect chemical signals released by other nerve cells

93
Q

State the function and example of:

Defensive proteins

A

Protection against disease

Antibodies combat bacteria and viruses

94
Q

Life would not be possible without _______, most of which are ________

A

Enzymes

Proteins

95
Q

Define:

Catalysts

A

Chemical agents that selectively speed up chemical reactions without being consumed by the reaction

96
Q

What are polymers of amino acids known as?

A

Polypeptides

97
Q

A protein consists of ___ or ____ ____________, each ______ and ______ into a specific three-dimensional structure

A

One
More polypeptides
Folded
Coiled

98
Q

What are amino acids?

A

Organic molecules possessing both carboxyl and amino groups

99
Q

What is the asymmetric carbon in the middle of an amino acid known as?

A

Alpha-carbon

100
Q

How many types of amino acids are there?

A

20

101
Q

What are the three types of amino acids?

A

Nonpolar, polar, and electrically charged

102
Q

Which amino acids are nonpolar? (9)

A

Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Phenylalanine, Tryptophan, Proline

103
Q

Which amino acids are polar? (6)

A

Serine, Threonine, Cysteine, Tyrosine, Asparagine, Glutamine

104
Q

What are the types of electrically charged amino acids? (2)

A

Acidic and Basic

105
Q

Which amino acids are electrically charged? (5)

A

Aspartic acid, Glutamic acid, Lysine, Arginine, Histidine

106
Q

Which electrically charged amino acids are acidic?

A

Aspartic acid and Glutamic acid

107
Q

Which electrically charged amino acids are basic?

A

Lysine, Arginine, and Histidine

108
Q

Name the amino acid:

Gly or G

A

Glycine

109
Q

Name the amino acid:

Ala or A

A

Alanine

110
Q

Name the amino acid:

Val or V

A

Valine

111
Q

Name the amino acid:

Leu or L

A

Leucine

112
Q

Name the amino acid:

Ile or I

A

Isoleucine

113
Q

Name the amino acid:

Met or M

A

Methionine

114
Q

Name the amino acid:

Phe or F

A

Phenylalanine

115
Q

Name the amino acid:

Trp or W

A

Tryptophan

116
Q

Name the amino acid:

Pro or P

A

Proline

117
Q

Name the amino acid:

Ser or S

A

Serine

118
Q

Name the amino acid:

Thr or T

A

Theonine

119
Q

Name the amino acid:

Cys or C

A

Cysteine

120
Q

Name the amino acid:

Tyr or Y

A

Tyrosine

121
Q

Name the amino acid:

Asn or N

A

Asparagine

122
Q

Name the amino acid:

Gln or Q

A

Glutamine

123
Q

Name the amino acid:

Asp or D

A

Aspartic acid

124
Q

Name the amino acid:

Glu or E

A

Glutamic acid

125
Q

Name the amino acid:

Lys or K

A

Lysine

126
Q

Name the amino acid:

Arg or R

A

Arginine

127
Q

Name the amino acid:

His or H

A

Histidine

128
Q

Name the abbreviations of amino acid:

Glycine

A

Gly or G

129
Q

Name the abbreviations of amino acid:

Alanine

A

Ala or A

130
Q

Name the abbreviations of amino acid:

Valine

A

Val or V

131
Q

Name the abbreviations of amino acid:

Leucine

A

Leu or L

132
Q

Name the abbreviations of amino acid:

Isoleucine

A

Ile or I

133
Q

Name the abbreviations of amino acid:

Methionine

A

Met or M

134
Q

Name the abbreviations of amino acid:

Phenylalanine

A

Phe or F

135
Q

Name the abbreviations of amino acid:

Tryptophan

A

Trp or W

136
Q

Name the abbreviations of amino acid:

Proline

A

Pro or P

137
Q

Name the abbreviations of amino acid:

Serine

A

Ser or S

138
Q

Name the abbreviations of amino acid:

Threonine

A

Thr or T

139
Q

Name the abbreviations of amino acid:

Cysteine

A

Cys or C

140
Q

Name the abbreviations of amino acid:

Tyrosine

A

Tyr or Y

141
Q

Name the abbreviations of amino acid:

Asparagine

A

Asn or N

142
Q

Name the abbreviations of amino acid:

Glutamine

A

Gln or Q

143
Q

Name the abbreviations of amino acid:

Aspartic acid

A

Asp or D

144
Q

Name the abbreviations of amino acid:

Glutamic acid

A

Glu or E

145
Q

Name the abbreviations of amino acid:

Lysine

A

Lys or K

146
Q

Name the abbreviations of amino acid:

Arginine

A

Arg or R

147
Q

Name the abbreviations of amino acid:

Histidine

A

His or H

148
Q

Name the amino acid with R group of:

H-

A

Glycine

149
Q

Name the amino acid with R group of:

CH3-

A

Alanine

150
Q

Name the amino acid with R group of:

(CH3)2CH-

A

Valine

151
Q

Name the amino acid with R group of:

(CH3)2CHCH2-

A

Leucine

152
Q

Name the amino acid with R group of:

CH3CH2CH(CH3)-

A

Isoleucine

153
Q

Name the amino acid with R group of:

CH3SCH2CH2-

A

Methionine

154
Q

Name the amino acid with R group of:

C6H5CH2-

A

Phenylalanine

155
Q

Name the amino acid with R group of:

C8H8NHCH2-

A

Tryptophan

156
Q

Name the amino acid with R group of:

-CH2CH2CH2

A

Proline

157
Q

Name the amino acid with R group of:

HOCH2-

A

Serine

158
Q

Name the amino acid with R group of:

(OHCH3)CH-

A

Threonine

159
Q

Name the amino acid with R group of:

HSCH2-

A

Cysteine

160
Q

Name the amino acid with R group of:

HOC6H4CH2-

A

Tyrosine

161
Q

Name the amino acid with R group of:

H2NC(O)CH2-

A

Asparagine

162
Q

Name the amino acid with R group of:

H2NC(O)CH2CH2-

A

Glutamine

163
Q

Name the amino acid with R group of:

O(-)C(O)CH2-

A

Aspartic acid

164
Q

Name the amino acid with R group of:

O(-)C(O)CH2CH2-

A

Glutamic acid

165
Q

Name the amino acid with R group of:

H3N(+)CH2CH2CH2CH2-

A

Lysine

166
Q

Name the amino acid with R group of:

H2NC(NH2(+))NHCH2CH2CH2-

A

Arginine

167
Q

Name the amino acid with R group of:

C3H2NHNH(+)CH2-

A

Histidine

168
Q

The group that differs on an amino acid is known as:

A

R group

169
Q

When two amino acids join by a dehydration reaction, what is the resulting covalent bond called?

A

Peptide bond

170
Q

What are the two ends of a polypeptide chain known as?

A 
Amino end (N-terminus)
Carboxyl end (C-terminus)
171
Q

True or False:

A polypeptide is a protein

A

False, the term polypeptide is not synonymous with the term protein

172
Q

A functional protein is ___ or more ____________ precisely _______, ______, and ______ into a ________ of unique shape

A 
One
Polypeptides
Twisted
Folded
Coiled
Molecule
173
Q

Describe:

Globular proteins

A

Roughly spherical proteins

174
Q

Describe:

Fibrous proteins

A

Proteins shaped like long fibers

175
Q

What does a ribbon model show?

A

Shows how the single polypeptide chain folds and coils to form the functional protein

176
Q

What do the yellow lines in a ribbon model represent?

A

Cross-linking bonds between the protein peptides that stabilizes its shape

177
Q

What does a space-filling model show?

A

Shows more clearly the globular shape seen in many proteins, as well as the specific three-dimensional structure unique to certain proteins

178
Q

What can mimic endorphins? Why?

A

Heroin, morphine, and other opiate drugs

They share a similar shape with endorphins

179
Q

What are the four levels of protein structure?

A

Primary, secondary, tertiary, quaternary

180
Q

Define:

Protein’s Primary Structure

A

The unique sequence of amino acids

181
Q

Define:

Protein’s Secondary Structure

A

The coils or folds that contribute to the protein’s overall shape

182
Q

What are the coils and folds in secondary structure of a protein a result of?

A

Hydrogen bonds

183
Q

What are the two main types of secondary structures?

A

Alpha helix and Beta pleated sheet

184
Q

Describe:

Alpha helix

A

A delicate coil held together by hydrogen bonding between every fourth amino acid

185
Q

Describe:

Beta pleated sheet

A

Two or more regions of the polypeptide chain lying side by side are connected by hydrogen bonds between parts of the two parallel polypeptide backbones

186
Q

Define:

Protein’s Tertiary Structure

A

The overall shape of a polypeptide resulting from interactions between the side chains (R groups) of the various amino acids

187
Q

What is one interaction that contributes to tertiary structure?

A

Hydrophobic interaction

188
Q

Describe:

Hydrophobic interaction

A

Amino acids with hydrophobic side chains end up in clusters at the core of the protein, out of contact with water

189
Q

In tertiary structure, the shape of a protein may be reinforce further by covalent bonds called:

A

Disulfide bridges

190
Q

Where do disulfide bridges form?

A

Form where two cysteine monomers (amino acids with sulfhydryl groups on side chains) are brought close together by the folding of the protein; the sulfur of the two cysteine bond together

191
Q

Define:

Protein’s Quaternary Structure

A

The overall protein structure that results from the aggression of these polypeptide subunits (some proteins consist of two or more polypeptide chains aggregated into one functional macromolecule)

192
Q

True or False:

Even a change in the primary structure can affect a protein’s shape and ability to function

A

True

193
Q

What is an example of the effects of the change in primary structure?

A

Sickle-cell disease; The substitution of valine for glutamic acid causes an exposed hydrophobic region in the secondary/tertiary structure or hemoglobin, which in turn causes crystallization into a fibre (causes the abnormal sickle shape)

194
Q

Define:

Denaturation

A

Protein unravelling and losing its native shape

195
Q

Define:

Chaperonins

A

Protein molecules that assist in the proper folding of other proteins

196
Q

What are chaperonins also known as?

A

Chaperone proteins

197
Q

When were the first 3-D structure for proteins worked out? For what?

A

1959

Hemoglobin and related protein

198
Q

What first made working out 3-D structures for proteins possible?

A

X-ray crystallography

199
Q

What is a newer method now used for working out the 3-D structure of proteins? What is different about it?

A

Nuclear magnetic resonance (NMR) spectroscope

Does not require protein crystallization

200
Q

What is the newest approach of figuring out the 3-D structure of proteins?

A

Bioinformatics

201
Q

Define:

Gene

A

A unit of inheritance that programs the amino acid sequence of a polypeptide

202
Q

DNA belongs to which group of compounds?

A

Nucleic Acids

203
Q

What are the two types of nucleic acids in living organisms? What is their function?

A 
Deoxyribonucleic acid (DNA) and Ribonucleic acid (RNA)
Enable living organisms to reproduce their complex components from one generation to the next
204
Q

State the flow of DNA to proteins (3)

A

DNA directs the synthesis of a type of RNA known as messenger RNA (mRNA)
The mRNA moves into the cytoplasm via the nuclear pore
The mRNA interacts with the cell’s protein-synthesizing machinery to direct production of a polypeptide, which folds into all or part of a protein

205
Q

Nucleic acids are macromolecules that exist as polymers called:

A

Polynucleotides

206
Q

What are the monomers of polynucleotides called?

A

Nucleotide

207
Q

Describe the structure of a nucleotide

A

Composed of three parts:
A nitrogenous base
A five-carbon sugar (pentose)
A phosphate group

208
Q

What is the portion of a nucleotide without the phosphate group called?

A

Nucleoside

209
Q

There are ___ families of nitrogenous bases:

A

Two

Pyrimidines and Purines

210
Q

Describe:

Pyrimidines

A

Have six-membered ring of carbon and nitrogen atoms

211
Q

Describe:

Purines

A

Larger, with a six membered ring fused to a five membered ring

212
Q

State the pyrimidines (3)

A

Cytosine (C)
Thymine (T)
Uracil (U)

213
Q

State the purines (2)

A

Adenine (A)

Guanine (G)

214
Q

What sugar is connected to the nitrogenous base in the nucleotides of RNA? DNA?

A

RNA: Ribose
DNA: Deoxyribose

215
Q

What is the difference between ribose and deoxyribose?

A

In deoxyribose, the second carbon in the ring lacks an oxygen atom

216
Q

True or False:

RNA is composed of two polypeptide chains

A

False, RNA is composed of one polypeptide chain while DNA is composed of two polypeptide chains

217
Q

What is the structure of DNA?

A

Double helix

218
Q

What are the two ends of nucleotide polymers known as? Why?

A

5’ and 3’ ends

One end has a phosphate attached to a 5’ carbon, while the other end has a hydroxyl group on a 3’ carbon

219
Q

The two sugar phosphate backbones of DNA run in ________ 5’ to 3’ directions from each other, referred to as:

A

Opposite

Antiparallel

My Packs: AP Biology (7 decks)

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