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Dental Admissions Test > Fundamentals of Biology > Flashcards

Fundamentals of Biology Flashcards

1
Q

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

A

hydrogen
oxygen
nitrogen

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2
Q

__ are molecules that contain more than one element

A

compounds

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3
Q

strong attractive forces that hold atoms within a molecule

A

intramolecular forces

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4
Q

force that exists between molecules

A

intermolecular forces

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5
Q

do intra- or intermolecular forces determine physical properties?

A

intermolecular

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6
Q

3 varieties of carbohydrates

A

monosaccharides
disaccharides
polysaccharides

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7
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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8
Q

5-carbon monosaccharides are called

A

pentoses

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9
Q

6-carbon monosaccharides are called

A

hexoses

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10
Q

a sugar molecule is alpha if the OH group points __ on 1C

A

down

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11
Q

a sugar molecule is beta if the OH group points __ on 1c

A

up

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12
Q

ribose is a

A

pentose monosaccharides

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13
Q

glucose and fructose are

A

hexose monosaccharides

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14
Q

glucose and fructose are __ of each other

A

isomers

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15
Q

what type of reactions bring monosaccharides together?

A

dehydration/condensation

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16
Q

what functional groups/atoms react in a dehydration/condensation reaction?

A

hydroxyl (OH) + hydrogen (H)

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17
Q

what is formed in a condensation reaction?

A

covalent bond

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18
Q

what is released in a condensation reaction?

A

H2O

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19
Q

what is opposite of condensation/dehydration reaction?

A

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

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20
Q

bond between a carbohydrate and another molecule

A

glycosidic

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21
Q

carbohydrates linked to lipids

A

glycolipids

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22
Q

carbohydrates linked to proteins

A

glycoproteins

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23
Q

the disaccharide __ is table sugar

A

sucrose

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24
Q

disaccharide of glucose and fructose

A

sucrose

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25
Q

disaccharide of galactose and glucose

A

lactose

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26
Q

disaccharide of 2 glucoses

A

maltose

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27
Q

__ may or may not have branching

A

polysaccharides

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28
Q

uses of polysaccharides

A

storage

structure

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29
Q

crucial storage polysaccharide in plants

A

starch

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30
Q

starch contains many __ monomers in linear and branched forms

A

glucose

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31
Q

linear plant starch

A

amylose

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32
Q

type of glycosidic bonds in amylose

A

a-1,4-glycosidic bonds (linear)

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33
Q

branched form of plant starch

A

amylopectin

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34
Q

type of glycosidic bonds in amylopectin

A

a-1,4-glycosidic (linear)

a-1,6-glycosidic (branches)

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35
Q

storage polysaccharide found in huans

A

glycogen

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36
Q

monomers in glycogen

A

glucose

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37
Q

is amylopectin or glycogen more branched?

A

glycogen

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38
Q

type of glycosidic bonds in glycogen

A

a-1,4-glycosidic (linear)

MANY a-1,6-glycosidic (branches)

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39
Q

which type of human tissues store glycogen?

A

liver (mostly)

muscles

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40
Q

name two a-glucose polysaccharides

A

starch

glycogen

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41
Q

structural polysaccharide in plant cell walls, wood, and paper

A

cellulose

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42
Q

cellulose is a __ polymer

A

glucose

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43
Q

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

A

b-1,4-glycosidic

allow cellulose to form linear strands that pack together in parallel

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44
Q

intermolecular force that holds adjacent cellulose strands together in parallel

A

H bonds

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45
Q

structure of cellulose gives it high __

A

rigidity

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46
Q

can humans digest cellulose?

A

no - passes thru digestive tract as fiber

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47
Q

chitin is a __ polysaccharide

A

structural

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48
Q

chitin is found in __

A

fungal cell walls

insect exoskeletons

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49
Q

chitin is a polysaccharide of __ monomers

A

N-acetylglucosamine

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50
Q

what type of bonds are in chitin?

A

b-1,4-glycosidic

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51
Q

chitin looks a lot like __

A

cellulose

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52
Q

name 2 beta-glucose polysaccharides

A

cellulose

chitin

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53
Q

protein polymers

A

polypeptides

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54
Q

polypeptide monomers

A

amino acid

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55
Q

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

A

H
NH2
COOH
R

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56
Q

how many different amino acids?

A

20

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57
Q

amino acids in a polypeptide are linked by __ covalent bonds

A

peptide

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58
Q

how do aas form peptide bonds?

A

dehydration/condensation

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59
Q

what type of reactions separate the aas in a polypeptide?

A

hydrolysis

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60
Q

a peptide bond is an __ bond involving aas

A

amide

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61
Q

amide/peptide bonds occur between __ and __ functional groups

A

NH2

COOH

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62
Q

what enzymes catalyze peptide bond formation?

A

peptidyl transferases

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63
Q

peptidyl transferases are __ transferases

A

aminoacyl

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64
Q

polypeptides have an __ and __ terminus

A

animo (N-)

carboxyl (C-)

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65
Q

primary protein structure

A

primary

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66
Q

all proteins have __ structure

A

primary

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67
Q

secondary protein strucutre

A

3D shape from intermolecular forces between the polypeptide backbone

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68
Q

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

A

polypeptide backbone

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69
Q

does secondary structure include interactions between R-group atoms?

A

no

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70
Q

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

A

secondary

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71
Q

most common type of intermolecular force for secondary structure

A

H-bonds

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72
Q

tertiary protein structure

A

3D protein structure due to non-covalent interactions between aa R-groups

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73
Q

common interactions between R-groups in tertiary strucutre

A 
ionic
hydrogen
dipole-dipole
van der Waal
hydrophobic
disulfide
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74
Q

“covalent exception in tertiary structure”

A

disulfide bonds

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75
Q

aas that cause disulfide bond formation

A

cysteine

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76
Q

quaternary protein structure

A

3D structure from grouping of 2 or more separate polypeptides

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77
Q

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

A

1 protein

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78
Q

3 structural classifications of proteins

A

fibrous
globular
intermediate

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79
Q

solubility of fibrous structural proteins

A

insoluble

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80
Q

fibrous structural proteins are long polymer __

A

fibers/sheets

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81
Q

__ form the structural components of cells

A

fibrous structural proteins

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82
Q

example of fibrous structural protein

A

collagen

83
Q

solubility of globular structural proteins

A

soluble

84
Q

__ structural proteins are folded tightly and perform many functions

A

globular

85
Q

example of globular structural protein

A

albumin

86
Q

solubility of intermediate structural proteins

A

soluble

87
Q

__ structural proteins are fiber-shaped and perform many functions

A

intermediate

88
Q

example of intermediate structural protein

A

fibrinogen

89
Q

2 compositional protein classifications

A

simple

conjugated

90
Q

simple protein compositions contain only __

A

amino acids

91
Q

conjugated protein compositions contain __

A

amino acids + non-protein components

92
Q

examples of conjugated proteins

A

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

93
Q

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

A

protein denaturation

94
Q

denatured proteins retain their __ structure

A

primary

95
Q

loss of __ leads to a loss of protein function

A

shape

96
Q

causes of protein denaturation

A

excess temperature
chemicals
pH change
radiation

97
Q

__ are molecules that increase reaction rates

A

catalysts

98
Q

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

A

spontaneity

99
Q

__ are not used up by the reactions they manipulate; the reaction does not change them

A

catalysts

100
Q

catalysts lower __ to speed reactions

A

activation energies

101
Q

catalysts do not affect the energy of __ or __

A

reactants

products

102
Q

enzymes

A

biological, globular protein (usually) catalysts

103
Q

substrates bind to enzymes at the __

A

active site

104
Q

are all enzymes proteins

A

no

ex. ribozymes

105
Q

active sites have unique properties and __

A

substrate specificity

106
Q

measures how efficient an enzyme is in converting substrate to product

A

specificity constant

107
Q

enzymes bind at the active site via the __ fit model

A

induced

108
Q

non-protein molecules that assist enzymes

A

cofactors

109
Q

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

A

electrons

110
Q

what are organic cofactors?

A

coenzymes

ex. vitamins

111
Q

inorganic cofactors are usually __

A

metal ions

112
Q

enzymes that are bound to their cofactor

A

holoenzymes

113
Q

an enzyme that is not bound to its cofactor

A

apoenzyme

114
Q

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

A

prosthetic groups

115
Q

enzyme efficiency is determined by __ and __

A

temperature

pH

116
Q

enzyme regulation where inhibitors compete with substrates for active sites

A

competitive inhibition

117
Q

we can outcompete a competitive inhibitor by adding more __

A

substrate

118
Q

what is enzyme saturation?

A

all active sites are occupied

119
Q

when an inhibitor binds to the allosteric site

A

noncompetitive inhibition

120
Q

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

A

allosteric site

121
Q

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

A

active site

122
Q

enzymes that have both an active site and an allosteric site

A

allosteric enzymes

123
Q

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

A

allosteric effector

124
Q

we cannot __ allosteric inhibitors by adding more substrate

A

outcompete

125
Q

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

A

noncompetitive inhibition

126
Q

substrate concentration at 1/2Vmax

A

Michaelis Constant (Km)

127
Q

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

A

small

128
Q

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

A

large

129
Q

in competitive inhibition, Km is raised but Vmax __

A

remains the same

130
Q

in noncompetitive inhibition, Km stays the same but Vmax

A

is lowered

131
Q

lipids are __, non-polar molecules

A

hydrophobic

132
Q

functions of lipids

A

store energy
insulation
cell membranes
endocrine lipids

133
Q

components of a triglyceride

A

three fatty acid chains attached to a glycerol backbone

134
Q

specialized fat cells that house triglycerides

A

adipocytes

135
Q

triglycerides are produced by __ reactions

A

dehydration/condensation

136
Q

which groups of which molecules react to form a triglyceride?

A

glycerol (H)

137
Q

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

A

ester

138
Q

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

A

hydrolysis

139
Q

fatty acids with no double bonds

A

saturated

140
Q

saturated fatty acids form __, __ chains

A

straight

stacked

141
Q

saturated fatty acids tend to be __ at room temp

A

solid

142
Q

fatty acids with 1 or more double bonds

A

unsaturated

143
Q

fatty acids with 1 double bond

A

monounsaturated

144
Q

fatty acids with 2 or more double bonds

A

2 or more

145
Q

cis-unsaturated fatty acids create __ in the fatty acid chain, so…

A

kinks

they do not pack tightly

146
Q

cis-unsaturated fats tend to be __ at room temp

A

liquid

147
Q

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

A

tightly

148
Q

unique type of lipid in cell membranes

A

phospholipids

149
Q

components of a phospholipid

A

2 fatty acids and 1 phosphate group attached to glycerol backbone

150
Q

amphipathic

A

having both hydrophobic and hydrophilic properties

ex. phosopholipids

151
Q

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

A

glycolipids

152
Q

cell membranes form through __ of phospholipids

A

self-assembly

153
Q

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

A

cholesterol

154
Q

cholesterol contains __ hydrocarbon rings and is also amphipathic

A

four

155
Q

factors that modulate membrane fluidity

A

temperature
cholesterol
degree of unsaturation in phospholipid fatty acid tails

156
Q

what maintains membrane fluidity in the cold?

A

increasing phospholipid unsaturation

cholesterol

157
Q

what maintains membrane fluidity in the heat

A

decreasing phospholipid unsaturation

cholesterol

158
Q

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

A

liver

diet

159
Q

cholesterol is a precursor to vitamin __ and __ acids

A

D

bile

160
Q

__ is a precursor to steroids

A

cholesterol

161
Q

general structure of a steroid

A

fused 4 ring structure - 3 cyclohexanes and 1 cyclopentane

162
Q

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

A

steroids

163
Q

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

A

lipoproteins

164
Q

lipoproteins contain a __ of phospholipids, cholesterol, and proteins

A

coat

165
Q

lipoproteins contains a __ that contains more cholesterol and triglycerides

A

lipid core

166
Q

low-density lipoproteins (LDLs)

A

have a low density of proteins are are generally considered unhealthy

167
Q

high-density lipoproteins (HDLs)

A

have a high density of proteins and are generally considered healthy

168
Q

waxes and carotenoids are __ derivatives

A

lipid

169
Q

esters of fatty acids and monohydroxy alcohols

A

waxes

170
Q

waxes are used as a __, protective coating

A

hydrophobic

171
Q

carotenoid structure

A

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

172
Q

carotenoid function

A

pigments

produce colors in plants and animals

173
Q

2 common nucleic acids

A

DNA

RNA

174
Q

__ have a pentose sugar attached to a nitrogenous base

A

nucleosides

175
Q

__ a pentose sugar attached to a nitrogenous base and a single phosphate group

A

nucleotide

176
Q

nucleic acids are polymers made of __

A

nucleotides

177
Q

nucleoside diphosphate

A

sugar
base
2 phosphates

178
Q

nucleoside triphosphate

A

sugar
base
3 phosphates

179
Q

4 possible bases of DNA nucleotide

A

adenine
thymine
cytosine
guanine

180
Q

4 possible bases of RNA nucleotide

A

adenine
uracil
cytosine
guanine

181
Q

purine

A

base with 2 rings

182
Q

pyrimidine

A

base with 1 ring

183
Q

adenine and guanine have 2 rings and are classified as __

A

purines

184
Q

cytosine, uracil, and thymine have 1 ring and are classified as __

A

pyrimidines

185
Q

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

A

RNA

186
Q

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

A

DNA

187
Q

RNA is more reactive than DNA because of its

A

2’ OH

188
Q

__ groups attach to the nucleotide sugar at the 5’ C

A

phosphate

189
Q

5’ __ of one nucleotide connects to the 3’ __ of another nucleotide in nucleic acids

A

phosphate

OH

190
Q

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

A

phosphodiester

191
Q

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

A

directionality

192
Q

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

A

nucleoside triphosphates

pyrophosphate

193
Q

DNA manifests as a __, __ helix

A

antiparallel

double-stranded

194
Q

A and T (or U) pair via __ hydrogen bonds

A

2

195
Q

C and G pair via __ H bonds

A

3

196
Q

RNA is usually __ stranded

A

single

197
Q

3 fundamental statements of cell theory

A

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

198
Q

does cell theory apply to viruses?

A

no - they are not living cells

199
Q

central dogma of genetics

A

information flows from DNA to RNA to proteins

200
Q

exception to the central dogma are __

A

prions

201
Q

prions

A

mis-folded proteins that cause other proteins to mis-fold

202
Q

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

A

RNA world

203
Q

RNA world hypothesis

A

self-replicating RNA molecules were the precursor to modern life

204
Q

2 central facts that support RNA world hypothesis

A

RNA is able to store genetic info like DNA

RNA is able to catalyze chemical reactions like proteins

Dental Admissions Test (3 decks)

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