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Flashcards in Chapter 3 Deck (263):
1

special case amino acids

Cysteine; Cys, C

Glycine; Gly, G

Proline; Pro, P

2

hydrophilic, uncharged amino acids

Serine; Ser, S

Threonine; Thr, T

Asparagine; Asn, N

Glutamine; Gln, Q

Tyrosine; Tyr, Y

3

electrically charged, hydrophilic amino acids

Arginine; Arg, R

Histidine; His, H

Lysine; Lys, K

Aspartic acid; Asp, D

Glutamic acid; Glue, E
 

4

nonpolar, hydrophobic amino acid

Alanine; Ala, A

Isoleucine; Ile, I

Leucine; Leu, L

Methionine; Met, M

Phenylalanine; Pha, F

Tryptophan; Trp, W

Valine; Val, V

5

linkages that form lipids

ester linkages
(are used to form these)

5

2-layered structure

bilayer

6

monomer

small molecule that can be combined with other similar molecules to form oligomers or polymers

7

R group
(synonym)

side chain
(synonym)

8

R group

distinguishing atoms of a particular amino acid

9

glycerol
(structure)

A image thumb
10

glycerol

3-Carbon alcohol with 3-OH groups
component of phospholipids and triglycerides

11

saturated fatty acid

fatty acid only containing single bonds within hydrocarbon chain

12

monosaccharide

monomer of carbohydrates
-a simple sugar

13

beta-pleated sheet

bonding between amino and carboxyl side groups resulting in _____

A image thumb
14

beta-pleated sheet

protein secondary structure resulting from regions of polypeptide running antiparallel to each other

15

quaternary structure

specific 3D arrangement of protein subunits
(e.g. full hemoglobin molecule consists of 4 subunits)

16

triglyceride

lipid containing a glycerol and 3 fatty acids

17

hexose

sugar containing 6 carbon atoms

18

glycosidic linkage

bonds between carbohydrates through an O atom

A image thumb
19

glycosidic linkage

linkage between carbohydrate molecules

20

optical isomers

mirror-image isomers

21

heat shock protein

chaperone protein expressed in cells exposed to environmental stressors (e.g. high/low temps)

22

carbohydrates

C, H, and O-containing compounds (in the ratio of 1:2:1)

22

carbohydrate examples (3)

sugars
starch
cellulose

22

chaperone

protein that guard other proteins by counteracting molecular interactions that threaten their 3D structure

23

disaccharide

carbohydrate consisting of two monosaccharides
-a simple sugar

25

bilayer

2-layered structure

25

condensation rxn

rxn in which two molecules are covalently joined with the release of a water molecule

26

fatty acid

molecule consisting of long nonpolar hydrocarbon chain(s) and a polar carboxyl group

found in many lipids

27

structural isomers

molecules consisting of the same types/numbers of atoms; atoms are bonded differently in each molecule

28

protein

long chain polymer consisting of amino acids; usually coiled into a compact molecule

28

secondary structure

localized protein folding, including alpha helices and beta (pleated) sheets

28

polysaccharide
(2 examples)

macromolecule consisting of many monosaccharides
cellulose
starch

29

primary structure

sequence of amino acids in a protein

30

phospholipid

lipid containing phosphate group

important constituent of cellular membranes

31

polymer

large molecule consisting of similar or identical subunits 

32

unsaturated fatty acid

fatty acid containing 1+ double bonds within hydrocarbon chain

33

tertiary structure

relative location of atoms/molecules within the 3D shape of a protein

OR relative shape of a protein

34

glucose

most common monosaccharide

34

isomers

molecules consisting of same types/numbers of atoms, but differences exist in bonding patterns

35

lipid
(and 5 examples)

nonpolar, hydrophobic molecules
-fats
-oils
-waxes
-steroids
-phospholipids

36

fat

triglyceride that is solid at room temp

37

macromolecule

large polymeric molecule

MW > 1,000

38

disulfide bridge

covalent bond between two sulfur atoms

links two molecules or remote parts of same molecule

40

pentose

sugar containing 5 carbon atoms

41

amphipathic

molecule having both hydrophobic and hydrophilic regions

42

hydrolysis reaction

chemical reaction that breaks a bond by inserting  components of water

44

oligosaccharide

polymer containing small number of monosaccharides

45

peptide linkage

bond between amino acids in protein

bond between carboxyl group and amino group w/ loss of a water molecule

45

peptide linkage
(details)

A image thumb
47

alpha helix

part of a protein's secondary structure; right handed spiral

bonds are between the H in the amino group and the O in the carboxyl group

48

alpha helix

hydrogen bonds between the H in the amino group and the O in the carboxyl group form a(n) _____

A image thumb
50

phospholipid bilayer

composes biological membranes

consists of 2 layers of amphipathic lipids; hydrophilic heads on outside of membrane, and hydrophobic tails on inside of membrane

51

side chain

distinguishing "R" group of an amino acid

52

functional group

characteristic combination of atoms/bonds that contribute to specific properties of a molecule

54

denaturation

loss of enzyme or nucleic acid molecular activity as a result of structural changes induced by environmental conditions

55

ester linkage

condensation reaction between carboxyl group of a fatty acid and a hydroxyl group of an alcohol

56

If 27 monomers of this general type (shown) were linked in a single-stranded chain, how many bonds would be formed, and what is the bond type called?

A. 27, peptide bond
B. 26, glycosidic linkage
C. 27, glycosidic linkage
D. 26, ester linkage
E. 28, peptide bond

Q image thumb

B

56

oil

triglyceride; liquid at room temp

58

This figure shows the testosterone molecule. Which of the following statements regarding these non-glycerol based lipids is false?

A. Non-glycerol based lipids are water soluble.
B. Carotenoids are light absorbing pigments.
C. Steroids are derived from cholesterol.
D. The vitamins A, D, E, and K are lipid soluble.
E. Waxes are formed by ester linkages between long chain fatty acids and long chain alcohols.

Q image thumb

A

58

Which of the five labeled bonds will be broken when this molecule undergoes hydrolysis?

A. 1
B. 2
C. 3
D. 4
E. 5

Q image thumb

C

60

This figure shows the relative amounts of substances found in living tissues. Which of the following statements about these substances is false?

A. The chemical behavior of molecules is determined by their functional groups.
B. Isomers are molecules with the same number and type of atoms arranged in different ways.
C. Hydrogen bonds are what hold monomeric substances in their polymeric form.
D. Water is required to break apart a polymer via hydrolysis.
E. Condensation refers to the formation of water as covalent bonds are formed between monomers (i.e., a polymer is formed).

Q image thumb

C

61

Which of the following statements about proteins is false? You may wish to refer to the generalized amino acid shown.

A. The sequence of amino acids is the primary structure of the protein.
B. Amino acids are isomers that are usually present in the D form in living cells.
C. A peptide linkage is a covalent bond that joins amino acids together.
D. The peptide backbone consists of the repeating sequence —N—C—C—.
E. The total number of different polypeptides containing seven amino acids is equal to 207.

Q image thumb

B

62

Which of the following statements about the protein structure shown is false?

A. It is an example of secondary protein structure.
B. This structure can involve more than one polypeptide.
C. It can be present in a polypeptide that also contains an α-helical structure.
D. It is maintained by hydrogen bonding between amino acid side chains.
E. The presence of this structure is determined by the protein's primary structure.

Q image thumb

D

64

Which of the following statements about the protein shown here is false?

A. This protein has a primary structure.
B. This protein has a secondary structure.
C. This protein has a tertiary structure.
D. This protein has a quaternary structure.
E. Heating this protein would cause it to lose its secondary and tertiary structures.

Q image thumb

D

65

Which statement about the two monosaccharides shown here is false?

A. These monosaccharides are isomers of a simple sugar with the formula C6H12O6.
B. These monosaccharides can form a disaccharide by a condensation reaction.
C. These monosaccharides could be joined together with a glycosidic linkage.
D. A β-glycosidic linkage will be formed between these monosaccharides.
E. In a disaccharide, these two monosaccharides could be joined at carbons 1 and 4.

Q image thumb

D

65

Which of the following statements about starch (shown) is false?

A. The subunits in starch are all glucose.
B. Starch is insoluble since it cannot bind to water.
C. Branching limits the hydrogen bonding that can occur between different starch molecules.
D. The degree of branching varies in different types of starch.
E. Starch is more similar to glycogen than it is to cellulose.

Q image thumb

B

67

Which of the following statements about the molecules shown is false?

A. They are all chemically modified carbohydrates.
B. Molecule 1 is a sugar phosphate.
C. Molecules 2 and 3 are amino sugars.
D. Chemically modified carbohydrates can be linked together.
E. They all are pentoses.

Q image thumb

E

68

In the formation of a triglyceride from the components shown (1 and 2), _______ molecule(s) of compound 1 combine(s) with _______ molecule(s) of compound 2 to form a triglyceride plus _______ molecule(s) of water.

A. 1; 1; 1
B. 1; 3; 1
C. 1; 3; 3
D. 3; 3; 3
E. 3; 1; 3

Q image thumb

C

69

Consider the two fatty acids shown (1 and 2). Which of the following statements regarding these fatty acids is false?

A. Fatty acid 1 contains a total of 16 carbons and 0 carbon–carbon double bonds.
B. Fatty acid 1 would be considered saturated.
C. Fatty acid 2 contains a carbon–carbon double bond.
D. Fatty acid 2 would be considered unsaturated.
E. Fatty acid 1 has a lower melting point than Fatty acid 2.

Q image thumb

E

71

Large molecules that contain carbon and are held together by covalent bonds are categorized as

A. proteins
B. polymers
C. nucleic acids
D. macromolecules
E. monomers

D

71

Consider the two labeled regions (1 and 2) of the phospholipid (phosphatidylcholine) shown here. Select the choice below that makes the following statement true: Region 1 is _______ and would form the _______ of a cell membrane; region 2 is _______ and would form the _______ of a cell membrane.

A. hydrophobic; interior; hydrophilic; surface
B. hydrophobic; surface; hydrophilic; interior
C. hydrophilic; surface; hydrophobic; surface
D. hydrophilic; surface; hydrophobic; interior
E. hydrophilic; interior; hydrophobic; interior

Q image thumb

D

73

The bonds that form between the monomers of polymeric macromolecules are ___ bonds.

A. hydrogen
B. peptide
C. disulfide
D. covalent
E. ionic

D

74

Quatenary structure of proteins refers to

A. the number and kind of polypeptide subunits the protein has.
B. the four-fold symmetry of the protein.
C. the arrangement of the protein's atoms in 3D space.
D. the lipids or carbohydrates taht are attached to the proteins.
E. whether the chain is an α helix or a β helix.

A

75

The side chain of leucine is a hydrocarbon. In a folded protein, where would you expect to find leucine?

A. in the interior of a cytoplasmic enzyme
B. on the exterior of a protein embedded in a membrane
C. on the exterior of a cytoplasmic enzyme
D. both a and b
E. both a and c

D

76

Which of the following functional groups is the most polar?

A. hydroxyl
B. aldehyde
C. keto
D. carboxylic acids
E. sulfhydryl

A

77

Aspartate and glutamate are highly soluble in water; therefore, they

A. are hydrophobic.
B. have sulfur atoms in their side chains.
C. have electrically charged side chains.
D. are nonpolar.
E. form only left-hand isomers.

C

78

During the formation of a peptide linkage, a(n) ___ is formed.

A. molecule of water
B. disulfide bridge
C. hydrophobic bond
D. hydrophilic bond
E. ionic bond

A

79

Amino acids can be classified by the

A. number of monosaccharides they contain.
B. number of carbon-carbon double bonds in their fatty acids.
C. number of peptide bonds they can form.
D. number of disulfide bridges they can form.
E. characteristics of their side chains, or "R" groups.

E

80

Which of the following does not represent a correct monomer/polymer pairing?

A. monosaccharide/polysaccharide
B. amino acid/protein
C. triglyceride/cellulose
D. nucleotide/nucleic acid
E. monosaccharide/oligosaccharide

C

81

The atoms that make up carbohydrates are

A.  C, H, and N.
B.  C and H.
C.  C, H, and P.
D.  C, H, and O.
E.   C, H, O, and N.

D

82

A fat contains fatty acids and

A. glycerol.
B. a base.
C. an amino acid.
D. a phosphate.
E. none of the above

A

83

Which of the following statements about the protein shown here is false?

A. This protein has a primary structure.
B. This protein has a secondary structure.
C. This protein has a tertiary structure.
D. This protein has a quaternary structure.
E. Heating this protein would cause it to lose its secondary and tertiary structures.

Q image thumb

D

84

Cholesterol is soluble in cholorform, an organic solvent, but it is not soluble in water. Based on this information, what class of biological macromolecules does cholesterol belong to?

A. oligosaccharides
B. enzymes
C. proteins
D. carbohydrates
E. lipids

E

85

Oils and fats

A. are phosopholipids.
B. all contain the same fatty acids.
C. are triglycerides.
D. are polar hydrocarbons.
E. have peptide bonds.

C

86

Which of the following statements about condensation reactions is not true?

A. Protein synthesis results from them.
B. Polysaccharide synthesis results from them.
C. They involve covalent bonds.
D. They consume water as a reactant.
E. Different condensation reactions produce different kinds of macromolecules. 

D

87

The most abundant molecule in the cell is

A. a carbohydrate.
B. a lipid.
C. a nucleic acid.
D. a protein.
E. water. 

E

88

All proteins

A. are enzymes.
B. consist of one or more polypeptide chains.
C. are amino acids.
D. have quaternary structures.
E. are more soluble in nonpolar solvents than in water. 

B

89

Which of the following statements about the primary structure of a protein is not true?

A. It may be branched.
B. It is held together by covalent bonds.
C. It is unique to that protein.
D. It determines the tertiary structure of the protein.
E. It is the sequence of amino acids in the protein. 

A

90

The amino acid leucine

A. is found in all proteins.
B. cannot form peptide linkages.
C. has a hydrophobic side chain.
D. has a hydrophilic side chain.
E. is identical to the amino acid lysine. 

C

91

All carbohydrates

A. are polymers.
B. are simple sugars.
C. consist of one or more simple sugars.
D. are found in biological membranes.
E. are more soluble in nonpolar solvents than in water. 

C

92

Which of the following is not a carbohydrate?

a. Glucose
b. Starch
c. Cellulose
d. Hemoglobin
e. Deoxyribose 

D

93

All lipids are

A. triglycerides.
B. polar.
C. hydrophilic.
D. polymers of fatty acids.
E. more soluble in nonpolar solvents than in water. 

E

94

The amphipathic nature of phospholipids is

A. determined by the fatty acid composition.
B. important in membrane structure.
C. polar but not nonpolar.
D. shown only if the lipid is in a nonpolar solvent.
E. important in energy storage by lipids. 

B

95

The quaternary structure of a protein

A. consists of four subunits—hence the name quaternary.
B. is unrelated to the function of the protein.
C. may be either alpha or beta.
D. depends on covalent bonding among the subunits.
E. depends on the primary structures of the subunits. 

E

96

3-Carbon alcohol with 3-OH groups
component of phospholipids and triglycerides

glycerol

97

alanine

hydrophobic

97

valine

hydrophobic

98

phenylalanine

hydrophobic

99

leucine

hydrophobic

100

isoleucine

hydrophobic

101

arginine

hydrophilic

positive

102

proline

special case

103

glycine

special case

104

cysteine

special case

105

tyrosine

hydrophilic

neutral

106

glutamine

hydrophilic

neutral

107

asparagine

hydrophilic

neutral

108

threonine

hydrophilic

neutral

109

serine

hydrophilic

neutral

110

glutamic acid

hydrophilic

negative

111

aspartic acid

hydrophilic

negative

112

lysine

hydrophilic

positive

113

histidine

hydrophilic

positive

115

aspartic acid
(structure)

A image thumb
115

glutamic acid
(structure)

A image thumb
115

tryptophan

hydrophobic

116

serine
(structure)

A image thumb
117

threonine
(structure)

A image thumb
118

asparagine
(structure)

A image thumb
119

glutamine
(structure)

A image thumb
120

tyrosine
(structure)

A image thumb
121

cysteine
(structure)

A image thumb
122

glycine
(structure)

A image thumb
123

proline
(structure)

A image thumb
124

alanine
(structure)

A image thumb
126

isoleucine
(structure)

A image thumb
127

leucine
(structure)

A image thumb
128

methionine
(structure)

A image thumb
129

phenylalanine
(structure)

A image thumb
130

tryptophan
(structure)

A image thumb
132

lysine
(structure)

A image thumb
132

valine
(structure)

A image thumb
134

histidine
(structure)

A image thumb
135

arginine
(structure)

A image thumb
136

valine
(abbreviation)

Val, V

137

tryptophan
(abbreviation)

Trp, W

138

phenylalanine
(abbreviation)

Phe, F

139

methionine
(abbreviation)

Met, M

140

leucine
(abbreviation)

Leu, L

141

isoleucine
(abbreviation)

Ile, I

142

alanine
(abbreviation0

Ala; A

143

proline
(abbreviation)

Pro, P

144

glycine
(abbreviation)

Gly, G

145

cysteine
(abbreviation)

Cys, C

146

tyrosine
(abbreviation)

Tyr, Y

147

glutamine
(abbreviation)

Gln, Q

148

asparagine
(abbreviation)

Asn, N

149

Q image thumb

valine
(structure)

150

threonine
(abbreviation)

Thr, T

151

serine
(abbreviation)

Ser, S

152

glutamic acid
(abbreviation)

Glu, E

153

aspartic acid
(abbreviation)

Asp, D

154

lysine
(abbreviation)

Lys, K

155

histidine
(abbreviation0

His, H

156

arginine
(abbreviation)

Arg, R

157

Q image thumb

tryptophan
(structure)

158

His, H

histidine
(abbreviation0

159

Lys, K

lysine
(abbreviation)

160

Asp, D

aspartic acid
(abbreviation)

161

Arg, R

arginine
(abbreviation)

162

Ser, S

serine
(abbreviation)

163

Thr, T

threonine
(abbreviation)

164

Asn, N

asparagine
(abbreviation)

165

Gln, Q

glutamine
(abbreviation)

166

Tyr, Y

tyrosine
(abbreviation)

167

Cys, C

cysteine
(abbreviation)

168

Gly, G

glycine
(abbreviation)

169

Pro, P

proline
(abbreviation)

170

Ala; A

alanine
(abbreviation0

171

Ile, I

isoleucine
(abbreviation)

172

Leu, L

leucine
(abbreviation)

173

Met, M

methionine
(abbreviation)

174

Phe, F

phenylalanine
(abbreviation)

175

Trp, W

tryptophan
(abbreviation)

176

Val, V

valine
(abbreviation)

177

Q image thumb

arginine
(structure)

178

Q image thumb

histidine
(structure)

179

Q image thumb

lysine
(structure)

180

Q image thumb

aspartic acid
(structure)

181

Q image thumb

glutamic acid
(structure)

182

Q image thumb

serine
(structure)

183

Q image thumb

threonine
(structure)

184

Q image thumb

asparagine
(structure)

185

Q image thumb

glutamine
(structure)

186

Q image thumb

tyrosine
(structure)

187

Q image thumb

cysteine
(structure)

188

Q image thumb

glycine
(structure)

189

Q image thumb

proline
(structure)

190

Q image thumb

alanine
(structure)

191

Q image thumb

isoleucine
(structure)

192

Q image thumb

leucine
(structure)

193

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methionine
(structure)

194

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phenylalanine
(structure)

195

Glu, E

glutamic acid
(abbreviation)

196

methionine

hydrophobic

197

bond between amino acids in protein

bond between carboxyl group and amino group w/ loss of a water molecule

peptide linkage

198

bonding between amino and carboxyl side groups resulting in _____

Q image thumb

beta-pleated sheet

199

bonds between carbohydrates through an O atom

Q image thumb

glycosidic linkage

200

C, H, and O-containing compounds (in the ratio of 1:2:1)

carbohydrates

201

carbohydrate consisting of two monosaccharides
-a simple sugar

disaccharide

202

chaperone protein expressed in cells exposed to environmental stressors (e.g. high/low temps)

heat shock protein

203

chemical reaction that breaks a bond by inserting  components of water

hydrolysis reaction

203

characteristic combination of atoms/bonds that contribute to specific properties of a molecule

functional group

204

composes biological membranes

consists of 2 layers of amphipathic lipids; hydrophilic heads on outside of membrane, and hydrophobic tails on inside of membrane

phospholipid bilayer

205

condensation reaction between carboxyl group of a fatty acid and a hydroxyl group of an alcohol

ester linkage

206

covalent bond between two sulfur atoms

links two molecules or remote parts of same molecule

disulfide bridge

207

distinguishing "R" group of an amino acid

side chain

207

distinguishing atoms of a particular amino acid

R group

208

ester linkages
(are used to form these)

linkages that form lipids

209

fatty acid containing 1+ double bonds within hydrocarbon chain

unsaturated fatty acid

210

fatty acid only containing single bonds within hydrocarbon chain

saturated fatty acid

212

Q image thumb

hydroxyl

213

Q image thumb

keto

214

Q image thumb

aldehyde

214

phosphate

A image thumb
215

Q image thumb

carboxyl

215

Q image thumb

amino

216

hydrogen bonds between the H in the amino group and the O in the carboxyl group form a(n) _____

Q image thumb

alpha helix

216

sulfhydryl

A image thumb
217

large molecule consisting of similar or identical subunits 

polymer

218

large polymeric molecule

MW > 1,000

macromolecule

220

linkage between carbohydrate molecules

glycosidic linkage

221

lipid containing a glycerol and 3 fatty acids

triglyceride

222

lipid containing phosphate group

important constituent of cellular membranes

phospholipid

223

localized protein folding, including alpha helices and beta (pleated) sheets

secondary structure

224

long chain polymer consisting of amino acids; usually coiled into a compact molecule

protein

225

loss of enzyme or nucleic acid molecular activity as a result of structural changes induced by environmental conditions

denaturation

226

macromolecule consisting of many monosaccharides
cellulose
starch

polysaccharide
(2 examples)

227

mirror-image isomers

optical isomers

228

molecule consisting of long nonpolar hydrocarbon chain(s) and a polar carboxyl group

found in many lipids

fatty acid

229

molecule having both hydrophobic and hydrophilic regions

amphipathic

230

molecules consisting of same types/numbers of atoms, but differences exist in bonding patterns

isomers

231

molecules consisting of the same types/numbers of atoms; atoms are bonded differently in each molecule

structural isomers

233

monomer of carbohydrates
-a simple sugar

monosaccharide

234

monomer of cellulose

glucose

235

monomer of glycogen

glucose

236

monomer of starch

glucose

237

most common monosaccharide

glucose

238

nonpolar, hydrophobic molecules
-fats
-oils
-waxes
-steroids
-phospholipids

lipid
(and 5 examples)

239

number of common amino acids

20

240

part of a protein's secondary structure; right handed spiral

bonds are between the H in the amino group and the O in the carboxyl group

alpha helix

241

polymer containing small number of monosaccharides

oligosaccharide

243

protein secondary structure resulting from regions of polypeptide running antiparallel to each other

beta-pleated sheet

245

protein that guard other proteins by counteracting molecular interactions that threaten their 3D structure

chaperone

246

relative location of atoms/molecules within the 3D shape of a protein

OR relative shape of a protein

tertiary structure

247

rxn in which two molecules are covalently joined with the release of a water molecule

condensation rxn

248

sequence of amino acids in a protein

primary structure

249

side chain
(synonym)

R group
(synonym)

250

specific 3D arrangement of protein subunits
(e.g. full hemoglobin molecule consists of 4 subunits)

quaternary structure

250

small molecule that can be combined with other similar molecules to form oligomers or polymers

monomer

251

sugar containing 6 carbon atoms

hexose

251

sugar containing 5 carbon atoms

pentose

253

sugars
starch
cellulose

carbohydrate examples (3)

255

triglyceride that is solid at room temp

fat

256

triglyceride; liquid at room temp

oil

257

hydroxyl

A image thumb
258

keto

A image thumb
259

aldehyde

A image thumb
260

Q image thumb

phosphate

261

carboxyl

A image thumb
262

amino

A image thumb
263

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sulfhydryl