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Biology 1406 > Unit 2 Exam (Chapters 5 and 27) > Flashcards

Unit 2 Exam (Chapters 5 and 27) Flashcards

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1
Q

All living things are made up of four classes of large biological molecules. Those four are

A

carbohydrates, lipids, proteins, and nucleic acids

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2
Q

Within cells, small organic molecules are joined together to form

A

larger molecules

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3
Q

Macromolecules

A

are large molecules composed of thousands of covalently connected atoms.
Carbohydrates, lipids, proteins, and nucleic acids.

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4
Q

Molecular structure and function are

A

inseparable

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5
Q

A polymer

A

is a long molecule consisting of many similar building blocks.
Ex. like 4 expo markers being put together and connected at each end making a long stick.

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6
Q

Monomers

A

are the small building-block molecules that combine and form polymers.
Ex. one expo marker

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7
Q

Three of the four classes of life’s organic molecules are polymers. These three are

A

Carbohydrates
Proteins
Nucleic Acids

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8
Q

A dehydration reaction

A

occurs when two monomers bond together through the loss/production of a water molecule.
-Building up.
Removing water causes things to build up and stick together.

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9
Q

Polymers are disassembled to monomers by

A

hydrolysis

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10
Q

Hydrolysis

A

a reaction that is essentially the reverse of the dehydration reaction.
-Breaking apart.
Adding water causes it to break a part. The breaking apart happens after you add a water molecule.

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11
Q

Each cell has thousands of different

A

macromolecules

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12
Q

Macromolecules vary among cells of an organism, vary more within a species, and

A

vary even more between species

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13
Q

An immense variety of polymers can be built from a small set of

A

monomers.

This is because of arrangement. Its like the alphabet and the 26 letters that create millions of different words.

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14
Q

Carbohydrates

A

include sugers and the polymers of sugars.

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15
Q

The simplest carbohydrates are

A

monosaccharides, or single sugars.

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16
Q

Disaccharides are

A

two monosaccharides

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17
Q

Carbohydrate macromolecules are

A

polysaccharides

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18
Q

Polysaccharides are

A

polymers composed of many sugar building blocks

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19
Q

Three Carbohydrates

A
  • Monosaccharides
  • Disaccharides
  • Polysaccharides
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20
Q

Sugars- Names end in

A

-ose

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21
Q

Monosaccharides

A

have molecular formulas that are usually multiples of CH2O

C and O will always have the same amount.
H is always double of what C and O are.

CH2O
1:2:1

C6H12O6
1:2:1

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22
Q

Glucose (C6H12O6) is

A

the most common monosaccharide.

-Vary in length, location of carbonyl, isomers

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23
Q

Monosaccharides Structure

A

CH2O

1:2:1

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24
Q

Monosaccharides are the

A

simplest

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25
Q

Monosaccharides Function

A
  • Major fuel for cells (food, energy)

- Raw material for building molecules (use them as bricks to make other molecules)

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26
Q

Though often Monosaccharides are drawn as linear skeletons,

A

aqueous solutions many sugars form rings.
When wet, they will form rings.
When dry, they form straight lines.

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27
Q

Two monosaccharides=

A

a disaccharide

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28
Q

A disaccharide is

A

formed when a dehydration reactions joins two monosaccharides

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29
Q

The covalent bond that joins two monosaccharides and forms a disaccharide is called a

A

glycosidic linkage

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30
Q

Disaccaride function

A

do not need to know or worry about!

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31
Q

Three Disaccaride structures

A

Glucose + Fructose = Sucrose
Glucose + Glucose = Maltose
Glucose + Galactose = Lactose

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32
Q

Glucose + Fructose =

A

Sucrose

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33
Q

Glucose + Glucose =

A

Maltose

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34
Q

Glucose + Galactose =

A

Lactose

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35
Q

Dehydration reaction in the synthesis of

A

Maltose

and in the synthesis of Sucrose as well

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36
Q

Polysaccharides

A

the polymers of sugars

they have storage and structural roles

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37
Q

Polysaccharides structure and function are determined by its

A

sugar monomers and the positions of glycosidic linkages

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38
Q

Storage Polysaccharide

Starch

A

Starch, a polysaccharide of plants, consists entirely of glucose monomers.
lots of glucose.

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39
Q

Starch structure

A

1-4 a(alpha) linkages
a helical shape.

Plants make starch made up of a alpha glucose

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40
Q

Starch Function

A

Storage.

Plants store surplus starch as granules within chloroplasts and other plastids

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41
Q

Amylose

A

a simple starch.

unbranched

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42
Q

Amylopectin

A

a complex starch.
a few branch points.

ex. brown rice, whole grains

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43
Q

Starch structure and function

A

structure- plants– alpha glucose

function- storage

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44
Q

Storage Polysaccharide

Glycogen

A

is a polysaccharide in animals.

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45
Q

Glycogen structure

A

all glucose monomers.

highly branched.

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46
Q

Glycogen Function

A

Storage
Humans and other vertebrates store glycogen mainly in liver and muscle cells.
Stores only last 24 hours.
(how we store our energy)

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47
Q

Glycogen structure and function

A

structure- animals- glucose

function- storage

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48
Q

Structural Polysaccharide

Cellulose

A

The polysaccharide cellulose is a major component of the tough wall of plant cells.
made up of hundreds of glucose that only plants make.

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49
Q

Cellulose structure

A

like starch, cellulose is a polymer of glucose, but the glycosidic linkages differ.
The difference is based on two ring forms for glucose: alpha (a) and beta (B).
They look a little different.

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50
Q

a (alpha) glucose

A

is starch

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51
Q

B (beta) glucose

A

is cellulose

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52
Q

Cellulose Structure and Function

A

structure- plants- B (beta) glucose

Function- structure- it makes cell walls

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53
Q

polymers with a (alpha) glucose are

A

helical shapes

Starches

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54
Q

polymers with B (beta) glucose are

A

straight

cellulose

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55
Q

In straight structures of polymers/polysaccharides

A

H atoms on one strand can bond with OH groups on other strands (hydrogen bonds).
Parallel cellulose molecules held together this way are grouped into microfibris which form strong building materials for plants.

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56
Q

Enzymes that digest starch by hydrolyzing a (alpha) linkages can’t

A

hydrolyze B (beta) linkages in cellulose

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57
Q

Cellulose in human food passes through the

A

digestive tract as insoluble fiber

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58
Q

Some microbes use

A

enzymes to digest cellulose

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59
Q

Many herbivores, from cows to termites, have

A

symbiotic relationships with those microbes that use enzymes to digest cellulose.

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60
Q

We can not digest

A

B (beta) linkages

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61
Q

Structural Polysaccharide

Chitin

A

Chitin, another structural polysaccharide, is found in the exoskeleton of anthropods.
(the crunch sound when you step on bugs?)

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62
Q

Chitin also provides

A

structural support for the cell walls of many fungi

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63
Q

Chitin function

A

structure

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64
Q

Chitin structure

A

don’t worry about? see picture on slide?

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65
Q

Lipids are

A

the one class of large biological molecules that do NOT form polymers

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66
Q

The unifying feature of lipids is having

A

little or no affinity for water.

None of lipids like water.

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67
Q

Lipids are hydrophobic because

A

they consist mostly of hydrocarbons, which form nonpolar covalent bonds

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68
Q

Most biologically important lipids

A

fats
phospholipids
steroids

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69
Q

Lipids do not have any

A

monomers

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70
Q

Lipids bond is called an

A

ester linkage bond

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71
Q

Fats

A

are constructed from two types of smaller molecules: glycerol and fatty acids

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72
Q

Glycerol is a

A

three-carbon alcohol with a hydroxyl group attached to each carbon

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73
Q

A fatty acid consists of

A

a carboxyl group attached to a long carbon skeleton

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74
Q

Fats separate from water because

A

water molecules form hydrogen bonds with each other and exclude the fats

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75
Q

Fats structure

A

in a fat, three fatty acids are joined to a glycerol by an ester linkage, creating a triacylglycerol or triglyceride.

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76
Q

ester linkage bond is like a

A

covalent bond

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77
Q

Bond between glycerol and 3 fatty acids is called an

A

ester linkage

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78
Q

Fatty acids vary in length (number of carbons) and in the number and

A

locations of double bonds

not al the same

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79
Q

Saturated Fatty acids

A

have the maximum number of hydrogen atoms possible and no double bonds

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80
Q

Unsaturated fatty acids

A

have one or more double bonds (cis)

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81
Q

Saturated fat

A 
all single bonds.
straight ones.
Solid at room temperature.
Bad for you.
They are packed together densely
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82
Q

Unsaturated fat

A 
double bond in it somewhere which creates a kink.
liquid at room temperature.
you want to eat these.
they are good for you.
healthiest.
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83
Q

Fats made from saturated fatty acids are called

A

saturated fats, and are solid at room temperature.

Most animal fats are saturated

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84
Q

Fats made from unsaturated fatty acids are called

A

unsaturated fats or oils, and are liquid at room temperature.
Plant fats and fish fats are usually unsaturated

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85
Q

A diet rich in saturated fats contributes to

A

cardiovascular disease through plague deposits

86
Q

Hydrogenation is

A

the process of converting unsaturated fats to saturated fats by adding hydrogen

87
Q

Hydrogenating vegetable oils also creates unsaturated fats with

A

trans double bonds

88
Q

These Trans fats may contribute more than

A

saturated fats to cardiovascular disease.
the body has no way of processing these.
really bad for us.
death if eat them

89
Q

Certain unsaturated fatty acids are not

A

synthesized in the human body.
these must be supplied in the diet.

these essential fatty acids include the omega-3 fatty acids, required for normal growth, and thought to provide protection against cardiovascular disease.
(fish oils is where we get them)

90
Q

Fats function

A

the major function of fats is energy storage.

91
Q

Humans and other mammals store their fat in

A

adipose cells.

92
Q

Adipose tissue also cushions

A

vital organs and insulates the body

93
Q

Fats structure and function

A

structure- glycerol + 3 fatty acids [saturated, unsaturated, trans fat]
function- energy storage, cushion organs

94
Q

Phospholipids structure

A

phospholipid is made up of
glycerol
two fatty acids
a phosphate group.

95
Q

In a phospholipid, the two fatty acid tails are

A

hydrophobic, but the phosphate group and its attachments form a hydrophilic head

96
Q

When phospholipids are added to water, they self-assemble into a bilayer, with the hydrophobic tails

A

pointing toward the interior.

this is important because it relates to the function.

97
Q

The structure of phospholipids results in

A

a bilayer arrangement found in cell membranes.

98
Q

all cell membranes are made up of

A

phospholipids

99
Q

Phospholipids function

A

phospholipids are the major component of all cell membranes

100
Q

Phospholipids structure and function

A

structure- a glycerol, 2 fatty acids, and a phosphate group

function- cell membranes

101
Q

Steroids structure

A

steroids are lipids characterized by a carbon skeleton consisting of four fused rings

102
Q

Steroids function

A 
cholesterol, an important steroid, is a component in animal cell membranes.
Many hormones (Estrogen, testosterone) are synthesized from cholesterol. (steroids).
103
Q

Although cholesterol is essential in animals,

A

high levels in blood contribute to cardiovascular disease.

104
Q

Need cholesterol so we can

A

build cell membranes and have steroids (estrogen, testosterone)

105
Q

Steroids structure and function

A

structure- four fused rings

function- cell membranes/hormones

106
Q

Proteins account for more than

A

50% of the dry mass of most cells.

This is important!!!

107
Q

Proteins have 8 functions

A
  1. Enzymatic
  2. Defense against foreign substances
  3. Storage
  4. Transport
  5. Hormonal
  6. Receptor
  7. Contractile/movement
  8. Structural
108
Q

Proteins can do a

A

wide variety of jobs

109
Q

Enzymatic proteins

A

speed up reactions.
Function- selective acceleration of chemical reactions.
example: digestive enzymes catalyze the hydrolysis of bonds in food molecules

110
Q

Defensive proteins

A

function- protect against disease

example: antibodies inactivate and help destroy viruses and bacteria

111
Q

Storage proteins

A

function- storage of amino acids
example: casein, the protein of milk, is the major source of amino acids for baby mammals. Plants have storage proteins in their seeds. Ovalbumin is the protein of egg white, used as an amino acid source for the developing embryo

112
Q

Transport proteins

A

function- transport of substances
examples: hemoglobin, the iron-containing protein of vertebrate blood, transports oxygen from the lungs to other parts of the body. other proteins transport molecules across cell membranes.

113
Q

Hormonal proteins

A

function- coordination of an organism’s activities
example: insulin, a hormone secreted by the pancreas, causes other tissues to take up glucose, thus regulating blood sugar concentration

114
Q

Receptor proteins

A

function- response of cell to chemical stimuli

example: receptors built into the membrane of a nerve cell detect signaling molecules released by other nerve cells

115
Q

Contractile and Motor proteins

A

function- movement
examples: motor proteins are responsible for the undulations of cilia and flagella. Actin and myosin proteins are responsible for the contraction of muscles

116
Q

Structural proteins

A

function- support
examples: keratin is the protein of hair, horns, feathers, and other skin appendages. Insects and spiders use silk fibers to make their cocoons and webs, respectively. Collagen and elastin proteins provide a fibrous framework in animal connective tissues.

117
Q

Protein’s monomer

A

amino acids

118
Q

Protein’s bond

A

peptide bond

119
Q

Enzymes

A

are a type of protein that acts as a catalyst to speed up chemical reactions

120
Q

Enzymes can

A

perform their functions repeatedly, functioning as workhorses that carry out the processes of life. (they can do the same job over and over again and never run out)

Never used up, not changed in a reaction.
Names end in –ase

121
Q

All proteins have a

A

unique 3 dimensional shape

122
Q

Polypeptides structure

A

Polypeptides are unbranched polymers built from the same set of 20 amino acids.

structure of an amino acid
bonds/polypeptide
primary-quaternary structure

123
Q

A protein is a

A

biologically functional molecule that consists of one or more polypeptides.
it works.

124
Q

Carbohydrate bond

A

glycosidic

125
Q

lipid bond

A

ester linkage

126
Q

protein bond

A

peptide bonds

127
Q

Amino acids link together and form

A

polypeptides

128
Q

Amino acids are a type of

A

monomer

129
Q

Amino acids are

A

organic molecules with carboxyl and amino groups

130
Q

Amino acids differ in their

A

properties due to differing side chains, called R groups

131
Q

Cells use 20 amino acids to make

A

thousands of proteins.

132
Q

they all have an amino group, carboxyl group, but the one different thing is the

A

R group (side chain)

133
Q

Amino acids are linked by

A

peptide bonds.

between a carboxyl terminus and amino terminus

134
Q

A polypeptide is a

A

polymer of amino acids

135
Q

Polypeptides range in length from a

A

few to more than a thousand monomers

136
Q

Each polypeptide has a unique linear sequence of amino acids, with

A

a carboxyl end (C-terminus) and an amino end (N-terminus)

137
Q

a dehydration reaction occurs when

A

a new peptide bond is forming?

138
Q

Polypeptide does NOT equal a

A

protein

139
Q

A functional protein consists of

A

one or more polypeptides precisely twisted, folded, and coiled into a unique shape

140
Q

Ribbon models and space filling models can

A

depict a protein’s conformation

141
Q

The sequence of amino acids determines a protein’s

A

three-dimensional structure

142
Q

A protein’s structure determines its

A

function

143
Q

Four levels of protein structure

A

Primary structure,
secondary structure,
tertiary structure,
quaternary structure

144
Q

The primary structure of a protein is its

A

unique sequence of amino acids

145
Q

Secondary structure, found in most proteins, consists of

A

coils and folds in the polypeptide chain.

a (alpha) helices and B (beta) pleated sheets

146
Q

Tertiary structure is

A

determined by interactions among various side chains (R groups)

147
Q

Quaternary structure results when a

A

protein consists of multiple polypeptide chains

148
Q

Primary structure

A

the sequence of amino acids in a protein, is like the order of letters in a long word.

telling how to build the molecule. the names.

149
Q

Primary structure is determined by

A

inherited genetic information

150
Q

The coils and folds of secondary structure result from

A

from hydrogen bonds between repeating constituents of the polypeptide backbone
(why/how they form)

151
Q

Typical secondary structures

A

a coil called an a (alpha) helix

a folded structure called a B (beta) pleated sheet

152
Q

Tertiary structure is determined by

A

interactions between R groups, rather than interactions between backbone constituents

153
Q

Hydrophobic R groups will orient toward

A

the interior

154
Q

Hydrophilic R groups will orient toward

A

the exterior

155
Q

Interactions between R groups include

A

hydrogen bonds
ionic bonds
hydrophobic interactions
van der Waals interactions

156
Q

Strong covalent bonds called disulfide bridges may

A

reinforce the protein’s structure

157
Q

At the point during the tertiary structure level,

A

many proteins are functionally complete, but not all

158
Q

Quaternary structure results when

A

two or more polypeptide chains form one macromolecule

159
Q

Collagen is a

A

fibrous protein consisting of three polypeptides coiled like a rope

160
Q

Hemoglobin is a

A

globular protein consisting of four polypeptides: two alpha and two beta chains

161
Q

During quaternary structure,

A

multiple subunits (polypeptides) have to come together

162
Q

A slight change in primary structure can affect a protein’s

A

structure and ability to function

genetic

163
Q

Sickle-cell disease, an inherited blood disorder, results from

A

a single amino acid substitution in the protein hemoglobin.

only 1 amino acid is wrong

164
Q

In addition to primary structure,

A

physical and chemical conditions can affect structure

165
Q

Alterations in pH, salt concentration, temperature, or other environmental factors can cause a protein to

A

unravel

166
Q

This loss of a protein’s native structure is called

A

denaturation.

this is really bad

167
Q

A denatured protein is biologically inactive

A

biologically inactive

168
Q

It is hard to predict a protein’s structure from its

A

primary structure.

Most proteins probably go through several stages on their way to a stable structure

169
Q

Chaperonins are

A

protein molecules that assist the proper folding of other proteins

170
Q

Chaperonins help

A

proteins, makes sure they fold correctly.

important job!!

171
Q

Diseases such as Alzheimer’s, Parkinson’s, and mad cow disease are associated with

A

misfolded proteins

172
Q

Nucleic acids

A

store, transmit, and help express hereditary information

173
Q

The amino acid sequence of a polypeptide is programmed by a unit of inheritance called a

A

gene

174
Q

Genes are made of DNA, a

A

nucleic acid made of monomers called nucleotides

175
Q

Genetic information flows

A

DNA&raquo_space; RNA&raquo_space; Protein

biology’s central dogma

176
Q

two types of nucleic acids

A 
Deoxyribonucleic acid (DNA)
Ribonucleic acid (RNA)
177
Q

Function of DNA

A

DNA provides directions for its own replication

DNA directs synthesis of messenger RNA (mRNA)

178
Q

Function of RNA

A

mRNA, controls protein synthesis (helps make proteins)

Protein synthesis occurs on ribosomes

179
Q

DNA function

A
  • replicate

- make mRNA

180
Q

RNA function

A

-protein synthesis

181
Q

Nucleic acids are polymers called

A

polynucleotides

182
Q

Nucleic acid monomers

A

nucleotides

183
Q

Each polynucleotide is made of monomers called

A

nucleotides

184
Q

Nucleic Acids/ Nucleotides structure

A

each nucleotide consists of
a nitrogenous base
a pentose sugar
and one or more phosphate group

185
Q

The portion of a nucleotide without the phosphate group is called a

A

nucleoside

186
Q

Two families of nitrogenous bases

can change

A

Pyrimidines

Purines.

187
Q

Pyrimidines

A

cytosine, thymine, and uracil.
have a single six-membered ring.
one ring

188
Q

Purines

A

adenine and guanine.
have a six-membered ring fused to a five-membered ring.
double/two rings

189
Q

In DNA, the sugar is

A

deoxyribose

190
Q

In RNA, the sugar is

A

ribose

191
Q

Nucleotide polymers are linked together to build a

A

polynucleotide

192
Q

Adjacent nucleotides are joined by covalent bonds that form between the

A

—OH group on the 3’ carbon of one nucleotide and the phosphate on the 5’ carbon on the next.

These links create a backbone of sugar-phosphate units with nitrogenous bases as appendages

193
Q

The sequence of bases along a DNA or mRNA polymer is

A

unique for each gene

194
Q

RNA molecules usually exist as

A

single polypeptide chains

195
Q

DNA molecules have

A

two polynucleotides spiraling around an imaginary axis, forming a double helix

196
Q

In the DNA double helix, the two backbones run in opposite 5’→ 3’ directions from each other, an arrangement referred to as

A

antiparallel

197
Q

One DNA molecule includes

A

many genes

198
Q

The nitrogenous bases in DNA pair up and

A

form hydrogen bonds: adenine (A) always with thymine (T), and guanine (G) always with cytosine (C)

199
Q

Adenine (A) always pairs up with

A

Thymine (T)

200
Q

Guanine (G) always pairs up with

A

Cytosine (C)

201
Q

The nitrogenous bases in DNA pairing up is called

A

complementary base pairing

202
Q

Complementary pairing can also occur between

A

two RNA molecules or between parts of the same molecule

203
Q

In RNA,

A

thymine is replaced by uracil (U) so A and U pair

204
Q

RNA

A

Guanine and cytosine

Adenine and Uracil

205
Q

DNA

A

Adenine and Thymine

Guanine and Cytosine

206
Q

The linear sequences of nucleotides in DNA molecules are passed from

A

parents to offspring

207
Q

Two closely related species are more similar in DNA than are

A

more distantly related species

208
Q

Molecular biology can be used to assess

A

evolutionary kinship

209
Q

Higher levels of organization result in the

A

emergence of new properties.

working way up levels of hierarchy

210
Q

Organization is the key to the

A

chemistry of life

Biology 1406 (53 decks)

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