Fundamentals of Bio/Chemistry Flashcards

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1
Q

any substance that takes up space and has mass is called _____

A

matter

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2
Q

matter is composed of what?

A

elements

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3
Q

an _____ has specific chemical and physical properties

A

element

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4
Q

an _____ is the smallest unit of matter that still retains all the chemical properties of an element

A

atom

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5
Q

can an atom break-down into something smaller, while still retaining the properties of the original element?

A

no

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6
Q

molecules result whenever _____ atoms join together

A

2 or more

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7
Q

_____ contain carbon atoms arranged as long chains or rings

A

organic molecules

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8
Q

what atoms does carbon tend to bond with in an organic molecule?

A

hydrogen; oxygen; nitrogen

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9
Q

_____ are molecules that contain more than one element

A

compounds (ex. H2O is a molecule/compound)

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10
Q

what are the strong attractive forces that hold atoms within a molecule?

A

intramolecular forces

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11
Q

which type of force exists between molecules?

A

intermolecular forces

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12
Q

which type of force is weaker… intra- or intermolecular?

A

intermolecular

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13
Q

which type of force (intra-/intermolecular) determines physical properties?

A

intermolecular

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14
Q

_____ are molecules that have the potential of bonding to other identical molecules through chemical reactions

A

monomers

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15
Q

_____ is the process when monomers bond together, and it forms _____

A

polymerization; polymers

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16
Q

_____ are substances that have a large # of monomers bonded together

A

polymers

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17
Q

what are the 3 varieties of carbohydrates?

A

monosaccharides; disaccharides; polysaccharides

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18
Q

monosaccharides have a ratio of precisely _____ to a water molecule, and they have the empirical formula _____

A

1 carbon; (CH2O)n

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19
Q

5 carbon monosaccharides are called _____

A

pentoses

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20
Q

6 carbon monosaccharides are called _____

A

hexoses

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21
Q

a sugar molecule is classified as alpha if the OH group points _____ on the first carbon

A

down

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22
Q

a sugar molecule is classified as beta if the OH group points _____ on the first carbon

A

up

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23
Q

ribose is a _____ sugar (monosaccharide)

A

pentose

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24
Q

glucose and fructose are _____ sugars (monosaccharides)

A

hexose

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25
Q

glucose and fructose are _____ of each other

A

isomers

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26
Q

what type of carbohydrate results when 2 monosaccharides bond together?

A

disaccharide

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27
Q

_____ bring monosaccharides together

A

dehydration/condensation reactions

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28
Q

what reacts with what in a dehydration/condensation reaction?

A

hydroxyl (OH) + hydrogen (H)

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29
Q

what is formed and what is released in a condensation/ dehydration/condensation reaction?

A

covalent bond formation; release of H2O

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30
Q

what is the opposite of a condensation/dehydration reaction - why?

A

hydrolysis reaction; adds H2O to a covalent bond to split monomers apart

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31
Q

what is the name of the bond that occurs when a carbohydrate bonds to another molecule?

A

glycosidic

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32
Q

carbohydrates linked to lipids are known as _____

A

glycolipids

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33
Q

carbohydrates linked to proteins are known as _____

A

glycoproteins

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34
Q

the disaccharide _____ is table sugar

A

sucrose

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35
Q

which disaccharide contains 1 glucose and 1 fructose?

A

sucrose

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36
Q

which disaccharide contains 1 galactose and 1 glucose?

A

lactose

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37
Q

which disaccharide contains 2 glucoses?

A

maltose

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38
Q

polysaccharides are long polymers of _____

A

monosaccharides

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39
Q

_____ may or may not have branching

A

polysaccharides

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40
Q

some polysaccharides are for _____, and others are for structure.

A

storage

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41
Q

_____ is a crucial storage polysaccharide in plants

A

starch

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42
Q

starch contains many _____ monomers in linear forms as well as branched forms

A

glucose

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43
Q

linear plant starch is called _____

A

amylose

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44
Q

what type of glycosidic bonds are in amylose?

A

α-1,4-glycosidic bonds

linear

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45
Q

what is amylopectin?

A

branched form of plant starch

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46
Q

what type of glycosidic bonds are in amylopectin?

A

α-1,4-glycosidic (linear)

α-1,6-glycosidic (branches)

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47
Q

_____ is a storage polysaccharide found in humans

A

glycogen

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48
Q

glycogen contains many _____ monomers

A

glucose

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49
Q

is amylopectin or glycogen more branched?

A

glycogen

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50
Q

what type of bonds does glycogen have?

A

α-1,4-glycosidic (linear)

many α-1,6-glycosidic (branches)

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51
Q

which type of human tissues store glycogen?

A

liver (mostly); muscles

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52
Q

name two alpha-glucose polysaccharides

A

starch, glycogen

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53
Q

_____ is a structural polysaccharide in plant cell walls, wood, and paper

A

cellulose

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54
Q

cellulose is a _____ polymer

A

glucose

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55
Q

what type of bonds does cellulose contain - what do they do?

A

β-1,4-glycosidic; allow cellulose to linear strands that pack together in parallel

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56
Q

what type of intermolecular force holds adjacent cellulose strands together in parallel?

A

hydrogen bonds

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57
Q

cellulose’s structure gives it a high _____

A

rigidity

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58
Q

can humans digest cellulose?

A

no - it passes through the digestive tract as fiber

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59
Q

chitin is a _____ polysaccharide

A

structural

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60
Q

chitin is found in _____ cell walls and _____ exoskeletons

A

fungal; insect

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61
Q

chitin is a structural polysaccharide of _____ monomers

A

N-acetylglucosamine

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62
Q

what type of bonds are in chitin?

A

β-1,4-glycosidic

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63
Q

chitin looks a lot like _____

A

cellulose

parallel strands cross-linked by H-bonds

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64
Q

name two beta-glucose polysaccharides

A

cellulose, chitin

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65
Q

proteins contain polymers called _____

A

polypeptides

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66
Q

polypeptides are polymers of _____ monomers

A

amino acid

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67
Q

in an amino acid, what 4 things is the central carbon bonded to?

A

H, NH2, COOH, R

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68
Q

how many amino acids are there?

A

20

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69
Q

amino acids in a polypeptide are linked by _____ covalent bonds

A

peptide

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70
Q

how do amino acids form peptide bonds with one another?

A

dehydration/condensation reactions

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71
Q

which type of reactions separate the amino acids of a polypeptide?

A

hydrolysis

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72
Q

a peptide bond is an _____ bond involving amino acids

A

amide

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73
Q

amide/peptide bonds occur between _____ and _____ functional groups

A

NH2; COOH

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74
Q

what enzymes catalyze peptide bond formation?

A

peptidyl transferases

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75
Q

peptidyl transferases are _____ transferases

A

aminoacyl

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76
Q

polypeptides have an _____ and _____ terminus

A

amino (N-); carboxyl (C-)

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77
Q

the _____ structure of a protein is its amino acid sequence

A

primary

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78
Q

all proteins have _____ structure

A

primary

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79
Q

the _____ structure of a protein is the 3D shape from intermolecular forces between the polypeptide backbone

A

secondary

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80
Q

the _____ is the amino acid structural features other than the R-group

A

polypeptide backbone

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81
Q

does secondary structure include interactions between R-group atoms?

A

no

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82
Q

which level of protein structure includes alpha helix and beta sheet?

A

secondary

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83
Q

what is the most common type of intermolecular force for secondary structure?

A

H-bonds

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84
Q

the _____ structure is the 3D structure due to non-covalent interactions between amino acid R-groups

A

tertiary

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85
Q

what are the common interactions between R-groups in tertiary structure?

A

ionic; hydrogen; dipole-dipole; van der Waal; hydrophobic; disulfide

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86
Q

what is the “covalent exception” in tertiary structure?

A

disulfide bonds

these are covalent

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87
Q

which amino acids allows disulfide bond formation?

A

cysteine

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88
Q

the _____ structure of a protein is the 3D structure from the grouping of two or more separate polypeptides

A

quaternary

89
Q

while there are multiple polypeptide chains in quaternary structure, they function as _____

A

1 protein

90
Q

what are 3 structural classifications of proteins?

A

fibrous; globular; intermediate

91
Q

fibrous structural proteins are (soluble/insoluble)

A

insoluble

92
Q

fibrous structural proteins are long polymer _____

A

fibers/sheets

93
Q

_____ form the structural components of cells

A

fibrous structural proteins

94
Q

what is an example of a fibrous structural protein?

A

collagen

95
Q

globular structural proteins are (soluble/insoluble)

A

soluble

96
Q

_____ structural proteins are folded tightly and perform many functions

A

globular

97
Q

what is an example of a globular structural protein?

A

albumin

98
Q

intermediate structural proteins are (soluble/insoluble)

A

soluble

99
Q

_____ structural proteins are fiber-shaped and perform many functions

A

intermediate

100
Q

what is an example of a intermediate structural protein?

A

fibrinogen

101
Q

what are 2 compositional protein classifications?

A

simple; conjugated

102
Q

simple protein compositions contain only _____

A

amino acids

ex: albumin

103
Q

conjugated protein compositions contain _____

A

amino acids + non-protein components

104
Q

what are some examples of conjugated proteins?

A

glycoproteins (mucin); metalloproteins (hemoglobin); lipoproteins (LDL/HDL)

105
Q

_____ causes proteins to lose their secondary, tertiary, and quaternary structures

A

protein denaturation

106
Q

denatured proteins retain their _____ structure

A

primary

107
Q

loss of _____ leads to a loss of protein function

A

shape

denaturation

108
Q

what are some causes of protein denaturation?

A

excess temperature, chemicals, pH changes, radiation

109
Q

_____ are molecules that increase reaction rates

A

catalysts

110
Q

despite speeding up reactions, catalysts do not affect the _____ of a reaction

A

spontaneity

111
Q

_____ are not used up by the reactions they manipulate, meaning the reaction does not change them

A

catalysts

112
Q

catalysts lower _____ to speed reactions

A

activation energies/transition state energies

113
Q

_____ do not change energy absorbing reactions to energy releasing ones, or vice versa

A

catalysts

114
Q

catalysts do not affect the energy of _____ or _____

A

reactants; products

115
Q

_____ are biological, globular protein (usually) catalysts

A

enzymes

116
Q

substrates bind to enzymes at the _____

A

active site

117
Q

not all enzymes are proteins - give an example of an RNA enzyme:

A

ribozymes

118
Q

active sites have unique properties and _____

A

substrate specificity

119
Q

the _____ measures how efficient an enzyme is in converting substrate to product

A

specificity constant

120
Q

enzymes bind at the active site via the _____ fit model

A

induced

121
Q

non-protein molecules that assist enzymes

A

cofactors

122
Q

cofactors usually help enzymes by donating/accepting some reaction component, like _____

A

electrons

123
Q

what are organic cofactors (e.g. vitamins)?

A

coenzymes

124
Q

inorganic cofactors are usually _____

A

metal ions

125
Q

_____ refer to enzymes that are bound to their cofactor

A

holoenzymes

126
Q

what is an apoenzyme?

A

an enzyme that is lacking (not bound to) its cofactor

127
Q

cofactors that tightly/covalently bind to their enzyme are known as _____

A

prosthetic groups

forms a holoenzyme

128
Q

enzyme efficiency is determined by _____ and _____

A

temperature; pH

129
Q

_____ is a form of enzyme regulation, where inhibitors compete with substrates for active sites

A

competitive inhibition

130
Q

we can outcompete a competitive inhibitor by adding more _____

A

substrate

131
Q

what is enzyme saturation?

A

all active sites are occupied

132
Q

_____ is when an inhibitor binds to the allosteric site

A

noncompetitive inhibition

133
Q

what is an allosteric site?

A

a different location that is not the active site of enzyme catalysis

134
Q

a noncompetitive inhibitor binding to the allosteric site modifies the _____ so that the substrate has reduced binding or cannot bind

A

active site

135
Q

enzymes that have both an active site and an allosteric site

A

allosteric enzymes

136
Q

a molecule that binds to an enzyme at a site other than the active site and affects its activity

A

allosteric effector

137
Q

we cannot _____ allosteric inhibitors by adding more substrate

A

outcompete

138
Q

the rate of enzyme catalysis is unaffected by increasing the substrate concentration in _____

A

noncompetitive inhibition

139
Q

_____ is the substrate concentration at 50% of Vmax

A

Michaelis Constant (Km)

140
Q

a _____ Km indicates that Vmax is reached at low substrate concentrations

A

small

141
Q

a _____ Km indicates that Vmax is reached at high substrate concentrations

A

large

142
Q

in competitive inhibition, Km is raised but Vmax _____

A

remains the same

143
Q

in noncompetitive inhibition, Km stays the same but Vmax _____

A

is lowered

144
Q

lipids are _____, non-polar molecules

A

hydrophobic

145
Q

_____ store energy; insulation; cell membranes; endocrine

A

lipids

146
Q

what are the components of a triglyceride?

A

three fatty acid chains attached to a glycerol backbone

147
Q

what are adipocytes?

A

specialized fat cells that house triglycerides

148
Q

triglycerides are produced by _____ reactions

A

dehydration/condensation

149
Q

which groups of which molecules react to form a triglyceride?

A

glycerol (H)

150
Q

what type of bonds exist between glycerol/fatty acids in a triglyceride?

A

ester

151
Q

addition of H2O to a triglyceride’s esters will break the fatty acids off the glycerol backbone by a _____ reaction

A

hydrolysis

152
Q

_____ fatty acids have no double bonds

A

saturated

153
Q

saturated fatty acids form _____, stacked chains

A

straight

154
Q

saturated fatty acids tend to be _____ at room temperature

A

solid

155
Q

_____ fatty acids can possess 1 (or more) double bonds

A

unsaturated

156
Q

_____ fatty acids have 1 double bond

A

monounsaturated

157
Q

polyunsaturated fatty acids have _____ double bonds

A

2 or more

158
Q

cis-unsaturated fatty acids create _____ in the fatty acid chain, meaning they do not pack tightly

A

kinks

159
Q

cis-unsaturated fats tend to be _____ at room temperature

A

liquid

160
Q

trans-unsaturated fatty acids pack together _____, and they are very bad for health

A

tightly

161
Q

_____ are a unique type of lipid (fat) in cell membranes

A

phospholipids

162
Q

what are the components of a phospholipid?

A

2 fatty acids and 1 phosphate group attached to 1 glycerol backbone

163
Q

phospholipids are _____, meaning they have both hydrophobic and hydrophilic properties

A

amphipathic

164
Q

_____ are like phospholipids but with a carbohydrate group rather than a phosphate group

A

glycolipids

165
Q

cell membranes form through _____ of phospholipids

A

self-assembly

166
Q

_____ is another class of lipid that makes up around 30-50% of a eukaryotic cell membrane

A

cholesterol

167
Q

cholesterol contains _____ hydrocarbon rings and is also amphipathic

A

four

168
Q

what are the factors that modulate membrane fluidity?

A

temperature; cholesterol; degree of unsaturation in phospholipid fatty acid tails

169
Q

what maintains membrane fluidity in the cold?

A

increasing phospholipid unsaturation; cholesterol

170
Q

what maintains membrane fluidity in the heat?

A

decreasing phospholipid unsaturation; cholesterol

171
Q

the _____ makes cholesterol, and we can also get it from the _____

A

liver; diet

172
Q

cholesterol is a precursor to vitamin _____ and _____ acids

A

D; bile

173
Q

_____ is a precursor to steroids

A

cholesterol

174
Q

describe the general structure of a steroid:

A

fused 4 ring structure (3 cyclohexanes & 1 cyclopentane)

175
Q

_____ are used as hormones and are a structural component of membranes (cholesterol)

A

steroids

176
Q

lipids are insoluble and must be transported through the blood by _____

A

lipoproteins

177
Q

lipoproteins contain a _____ of phospholipids, cholesterol, and proteins

A

coat

178
Q

lipoproteins contain a _____ that contains more cholesterol and triglycerides

A

lipid core

179
Q

_____ (lipoproteins) have a low density of proteins and are generally considered unhealthy

A

low-density lipoproteins (LDLs)

180
Q

_____ (lipoproteins) have a high density of proteins and are generally considered to be healthy

A

high-density lipoproteins (HDLs)

181
Q

waxes & carotenoids are _____ derivatives

A

lipid

182
Q

esters of fatty acids and monohydroxy alcohols

A

waxes

183
Q

waxes are used as a _____, protective coating

A

hydrophobic

184
Q

carotenoid structure:

A

fatty acid carbon chains with conjugated double bounds and 6-membered rings at each end

185
Q

carotenoid function:

A

pigments, which produce colors in plants and animals

186
Q

what are 2 common nucleic acids to know?

A

DNA; RNA

187
Q

_____ have a pentose sugar attached to a nitrogenous base

A

nucleosides

188
Q

a _____ is a pentose sugar attached to a nitrogenous base and a single phosphate group

A

nucleotide

189
Q

nucleic acids are polymers made of _____

A

nucleotides

190
Q

nucleoside di- or triphosphates have more than 1 _____ group

A

phosphate

191
Q

what are the 4 possible bases of a DNA nucleotide?

A

adenine, thymine, cytosine, guanine

192
Q

what are the 4 possible bases of a RNA nucleotide?

A

adenine, uracil, cytosine, guanine

193
Q

nucleotides can be further categorized depending on their nitrogen base as a _____ or _____

A

purine; pyrimidine

194
Q

_____ bases have 2 rings

A

purine

195
Q

_____ bases have 1 ring

A

pyrimidine

196
Q

Adenine and Guanine have 2 rings and are classified as _____

A

PURines

PUR As Gold

197
Q

Cytosine, Uracil, and Thymine have 1 ring and are classified as _____

A

pyrimidines

CUT the PY

198
Q

_____ nucleotides have ribose sugars with a hydroxyl on the 2’ carbon

A

RNA

199
Q

_____ nucleotides have deoxyribose sugars without a hydroxyl on the 2’ carbon

A

DNA

200
Q

RNA is more reactive (less stable) than DNA because of its _____

A

2’ hydroxyl

201
Q

_____ groups attach to the nucleotide sugar at the 5’ carbon

A

phosphate

202
Q

5’ _____ of one nucleotide connect to the 3’ _____ of another nucleotide in nucleic acids

A

phosphates; hydroxyl

203
Q

bonding between a 5’ phosphate and a 3’ hydroxyl creates a _____ bond in nucleic acids

A

phosphodiester

204
Q

what creates the sugar-phosphate backbone of nucleic acid?

A

phosphodiester bonds

205
Q

nucleic acids have _____, with a 5’ and 3’ end

A

directionality

206
Q

_____ add to growing nucleic acid polymers by losing two phosphates (as _____)

A

nucleoside triphosphates; pyrophosphate

207
Q

DNA manifests as a _____, _____ helix

A

antiparallel; double-stranded

208
Q

purines can only H-bond to _____

A

pyrimidines

209
Q

pyrimidines can only H-bond to _____

A

purines

210
Q

adenine and thymine (or uracil) pair together via _____ hydrogen bonds

A

2

211
Q

cytosine and guanine pair together via _____ hydrogen bonds

A

3

212
Q

unlike DNA, RNA is usually _____ stranded

A

single

213
Q

what are the 3 fundamental statements of the cell theory?

A

all lifeforms have 1 or more cells; cells are the most simple unit of life; cells come from other cells

214
Q

does the cell-theory apply to viruses?

A

no - they are not living cells

215
Q

the central dogma of genetics states that information flows from _____ to _____ to _____

A

DNA; RNA; proteins

216
Q

an exception to the central dogma of genetics are _____, mis-folded proteins that cause other proteins to mis-fold

A

prions

217
Q

what is the hypothesis for the creation of the first cell as we know it?

A

the RNA world hypothesis

218
Q

the RNA world hypothesis suggests that self-replicating _____ molecules were the precursor to current life

A

RNA

219
Q

what are 2 central facts that support the RNA world hypothesis?

A

RNA can: store genetic information like DNA; catalyze chemical reactions like proteins