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BI173—Cell & Organismal Biology > Exam 1 > Flashcards

Exam 1 Flashcards

1
Q

define hydroxyl group

A

C single bonded to OH

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2
Q
A

hydroxyl group

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3
Q

“alcohol”

A

hydroxyl group

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4
Q

define carbonyl group

A

C double bonded to O and to 2 other atoms

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5
Q
A

carbonyl group

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6
Q

“ketone/ketoses”

“aldehyde/aldoses”

A

carbonyl group

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7
Q

ketone vs aldehyde

A

ketone has C bonded to 2 C and double bonded to O

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8
Q

sugars & acetone have ______ groups

A

carbonyl

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9
Q

define carboxyl group

A

C double bonded to O, to OH, and to something else

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10
Q
A

carboxyl group

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11
Q

“organic acids”

A

carboxyl

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12
Q

ionized form of carboxyl group

A

H+ breaks off of the hydroxide, leaving O-

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13
Q

define amino group

A

N bound to 2 H and one C

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14
Q
A

amino group

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15
Q

ionized form of amino group

A

a H+ binds to N, making N+ (then N is bound to 3 H)

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16
Q

define sulfhydryl group

A

SH bound to chain

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17
Q
A

sulfhydryl group

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18
Q

“thiol”

A

sulfhydryl group

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19
Q

define phosphate group

A

P bound to 4 O with 3 single bonds and 1 double bond; 2 O- are included

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20
Q
A

phosphate group

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21
Q

allows molecules to react with water, releasing energy

A

phosphate groups

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22
Q

define methyl group

A

C bound to 3 H

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23
Q
A

methyl group

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24
Q

Affects expression of genes & sex hormones

A

methyl groups

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25
Q

elements that comprise 96% of living matter

A

carbon

hydrogen

oxygen

nitrogen

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26
Q

4 major properties of water

A
  1. cohesive behavior
  2. ability to moderate temperature (high specific heat)
  3. expansion upon freezing
  4. versatility as a solvent
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27
Q

why is cohesive behavior important in water?

A

allows water to flow against gravity in plants

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28
Q

define specific heat

A

amt of heat that must be absorbed/lost for 1 g of a substance to change temp by 1 degree C

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29
Q

2 properties of water that help organisms maintain stable temp

A

high specific heat

evaporative cooling

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30
Q

water reaches greatest density at ___ degrees C

A

4

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31
Q

if ice sank…

A

all bodies of water would eventually freeze

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32
Q

define hydration shell

A

when an ionic compound is dissolved, each ion is surrounded by a sphere of water molecules

(due to hydrogen bonds; hydrogens attracted to anions, oxygen attracted to cations)

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33
Q

explain dissociation of water

A

loses H+ — becomes OH- (hydroxide)

gains H+ — becomes H3O+ (hydronium)

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34
Q

______ protect organisms from extremes of pH

A

buffers

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35
Q

most biological fluids are between ___-___ pH

A

6-8

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36
Q

study of compounds containing carbon

A

organic chemistry

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37
Q

structure of carbon

protons

valence electrons

A

6

4

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38
Q

In molecules w/ multiple carbons, each carbon bonded for 4 other atoms has a _______ shape

A

tetrahedral

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39
Q

In molecules w/ 2 atoms joined by a double bond, the atoms joined are __________ as the carbon

A

in the same plane

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40
Q

define hydrocarbons

A

organic molecules only consisting of C and H

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41
Q

________ undergo reactions to release large amounts of energy

A

hydrocarbons

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42
Q

same molecular formula, but different structure & properties

A

isomers

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43
Q

3 types of isomers

A

structural

geometric/cis-trans

enantiomers

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44
Q

what are structural isomers?

A

different covalent arrangements - different shape

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45
Q

what are geometric isomers?

what do cis and trans mean?

A
  • same covalent bonds, but different structural arrangement
    • Cis - “x” atoms on same side
    • Trans - “x” atoms on opposite sides
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46
Q

what are enantiomers?

A

isomers that are mirror images of one another

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47
Q

examples of enantiomers

A

S ibuprofen works, R ibuprofen does not

R albuterol works, S albuterol does not

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48
Q

components of organic molecules most involved in chemical reactions

A

functional groups

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49
Q

define polymers

A

long chains of monomers

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50
Q

macromolecules are made of…

A

polymers

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51
Q

only non-macromolecule biomolecule

A

lipids

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52
Q

explain synthesis of polymers

A
  • Dehydration reaction - 2 monomers bind through loss of a water molecule
    • OH and H (on each monomer) bind to form water; water is released, and monomers are allowed to bind
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53
Q

explain breakdown of polymers

A
  • Hydrolysis - disassembly of polymers with addition of water - reverse of dehydration reaction
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54
Q

lipids consist mainly of…

A

hydrocarbons

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55
Q

most biologically important lipids

A

fats

phospholipids

steroids

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56
Q

components of fats

A

glycerol

fatty acids

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57
Q

what is a glycerol?

A

3-carbon alcohol with hydroxyl group attached to each carbon

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58
Q

what is a fatty acid?

A

carboxyl group attached to long carbon skeleton

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59
Q

explain saturated fatty acids

shape?

state?

source?

A

every available area on C is linked to H (all single bonds)

straight shape

solid at room temp

most animal fats

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60
Q

explain unsaturated fatty acids

shape?

state?

source?

A

have 1+ double bonds between C - prevent saturation with H

bent shape

liquid at room temp (“oils”)

most plant and fish fats

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61
Q

major functions of fats

A

energy storage

cushioning

insulation

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62
Q

components of phospholipids

A

2 fatty acids & a phosphate group attached to a glycerol

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63
Q

natural arrangement of phospholipids

A

bilayer

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64
Q

components of steroids

A

Lipids with carbon skeleton consisting of 4 fused rings

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65
Q

functions of cholesterol

A

component of animal cell membranes & precursor from which all other steroids are synthesized

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66
Q

covalent bond unique to lipids

connects glycerol to fatty acids

A

ester linkage

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67
Q

most basic formula of monosaccharides

A

CH2O

68
Q

monosaccharides classified by…

A

location of carbonyl group & number of carbons in skeleton

69
Q

Glucose + glucose =

A

maltose

70
Q

glucose + fructose =

A

sucrose

71
Q

covalent bond between monosaccharides

A

glycosidic linkage

72
Q

storage polysaccharide in plants

A

starch

73
Q

starch is stored as…

A

granules in chloroplasts & other plastids

74
Q

simplest starch

A

amylose

75
Q

animal storage of polysaccharides

A

glycogen

76
Q

major component of tough wall of plant cells

A

cellulose

77
Q

how is cellulose structured differently from starch?

A

OH side of the glucose is flipped on every other one

78
Q

where is chitin found?

A

exoskeleton of arthropods (embedded in proteins)

cell walls of fungi

79
Q

in aqueous solutions, most sugars form…

A

rings

80
Q

function of nucleic acids

A

Store, transmit & help express genetic information

81
Q

monomers of nucleic acids

A

nucleotides

82
Q

functions of DNA

A

includes directions for its own replication

directs synthesis of mRNA

controls protein synthesis (gene expression)

83
Q

function of mRNA

A

interacts with ribosomes to direct production of a polypeptide

84
Q

polymers of nucleic acids

A

polynucleotides

85
Q

components of nucleotides

A

a nitrogenous base, a pentose sugar, and 1+ phosphate groups

86
Q

what is a nucleoside?

A

portion of a nucleotide w/o the phosphate

87
Q

pentose sugar in DNA & RNA

A

dna - deoxyribose

rna - ribose

88
Q

2 families of nucleotides & their structures

A
  • Pyrimidines - cytosine, thymine, uracil - single 6-membered ring (smaller)
  • Purines - adenine, guanine - 6-membered ring fused to a 5-membered ring (larger)
89
Q

linkages of nucleic acids

A

phosphodiester bonds

90
Q

sugar-phosphate forms the _______ of DNA while the nitrogenous bases are ________

A

backbone

appendages

91
Q

codon

A

3 bases coding for 1 amino acid

92
Q

which directions are genes read in?

A

5 prime to 3 prime

93
Q

basic structure of DNA

A

Double helix - 2 polynucleotides spiraling around an imaginary axis - backbones run in opposite directions (antiparallel)

94
Q

__ hydrogen bonds between A & T

__ hydrogen bonds between C & G

A

2

3

95
Q

define protein

A

biologically functional molecule consisting of 1+ polypeptides

96
Q

define polypeptide

A

unbranched polymers built from amino acids

97
Q

2 ends of a polypeptide

A

carboxyl end (c-terminus)

amino end (n-terminus)

98
Q

structure of an amino acid

A

amino and carboxyl groups bound by an alpha carbon

unique R group

99
Q

bonds used in proteins

A

peptide bonds

100
Q

proteins account for >__% of dry mass of cells

A

50

101
Q

major functions of proteins (8)

A
  • Enzymes - catalyze chemical reactions
  • Defense - ex antibodies
  • Storage - store amino acids - ex casein, ovalbumin
  • Transport - ex hemoglobin, transport proteins
  • Cellular communication - ex hormones, receptor proteins
  • Movement - contractile & motor proteins - ex cilia, flagella, actin, myosin
  • Structural support - ex keratin, collagen, elastin
  • Gene regulation
102
Q

what is primary structure?

A

unique sequence of amino acids - determined by genetic info

103
Q

what is secondary structure?

A

coils (helices) & folds (pleated sheets) in polypeptide chain

104
Q

what is tertiary structure?

A

overall shape, resulting from interactions among various side chains (R groups) rather than backbone constituents

105
Q

what is quaternary structure?

A

when a protein consists of multiple polypeptide chains folded together (does not occur in all proteins)

106
Q

what allows hydrogen bonding in polypeptides?

A

Backbone of the chains have O bound to C (-) and H bound to O (+) at different spots

107
Q

hydrogen bonding between repeating constituents of the polypeptide backbone

A

secondary structure

108
Q

interactions among various side chains (R groups)

A

tertiary structure

109
Q

tertiary structure includes which types of bonds?

A

hydrogen bonds

ionic bonds

hydrophobic interactions (cluster on the inside of the protein)

van der waals interactions

110
Q

strong covalent bonds that reinforce protein’s structure

A

disulfide bridges

111
Q

fibrous protein consisting of 3 polypeptides coiled like rope

A

collagen

112
Q

hemoglobin consists of…

A

4 polypeptides (2 alpha and 2 beta subunits)

113
Q

begins with a specific molecule (substrate) & ends with a product

A

metabolic pathway

114
Q

energy is released by breaking down complex molecules

A

catabolic pathway

115
Q

consumes energy in order to build complex molecules from simpler ones

A

anabolic pathway

116
Q

study of how energy flows through living organisms

A

bioenergetics

117
Q

define energy

A

capacity to cause change

118
Q

define thermal energy

A

kinetic energy associated with random movement of atoms/molecules

119
Q

define heat

A

thermal energy transfer between objects

120
Q

define potential energy

A

energy that matter possesses because of its location or structure

121
Q

define chemical energy

A

potential energy available for release in a chemical reaction

122
Q

study of energy transformation

A

thermodynamics

123
Q

energy of the universe is constant

A

1st law of TD

124
Q

During every transfer of energy, some energy is unusable and “lost” as ______

A

thermal energy

125
Q

every transfer of energy increases the entropy of the universe

A

2nd law of TD

126
Q

define entropy

A

measure of randomness/molecular disorder

measure of thermal energy

not available to use in work

127
Q

examples of entropy increasing

A

increases as water boils

as salt dissolves in water

as we digest complex molecules

128
Q

define spontaneous processes

A

occur w/o energy input

energetically favorable

129
Q

example of a spontaneous process

A

water running down a hill

130
Q

processes that decrease entropy are _________; occur only if energy is provided

A

nonspontanteous

131
Q

why don’t organisms violate 2nd law?

A

Entropy may decrease in a particular system, as long as the total entropy of the system’s surroundings (universe) increases

132
Q

________________ of a reaction tells us whether or not the reaction occurs spontaneously

A

Free-energy change (ΔG)

133
Q

energy that can do work

measure of a system’s instability

tendency to change to a more stable state

A

Gibbs free energy

134
Q

ΔG =

A

ΔH - TΔS

135
Q

​​ΔG is ________ for all spontaneous processes

0 or ______ ΔG requires energy

A

negative for spontaneous processes

0 or positive requires energy

136
Q

define equilibrium

A

state of maximum stability

137
Q

only an ______ system can reach equilibrium

A

isolated

138
Q

define exergonic reactions

A

spontaneous

becomes more stable

net release of free energy

139
Q

define endergonic reactions

A

nonspontaneous

becomes less stable

absorbs free energy from its surroundings

140
Q

composition of ATP

A

ribose (sugar)

adenine (nitrogenous base)

3 phosphate groups

141
Q

define phosphorylation

A

the 3rd phosphate is transferred to another molecule (the phosphorylated intermediate)

142
Q

ATP powers cellular work by…

A

coupling exergonic reactions with endergonic reactions

143
Q

overall, coupled reactions are…

A

exergonic (ΔG is negative)

144
Q

exergonic = (-/+) ΔG

A

negative

145
Q

endergonic = (-/+) ΔG

A

positive

146
Q

3 main kinds of cellular work

A
  • Chemical - pushing endergonic reactions
  • Transport - pushing substances against direction of spontaneous movement (gradient)
  • Mechanical - ex contraction of muscle cells
147
Q

Energy to phosphorylate ADP comes from…

A

catabolic reactions in the cell

148
Q

define enzymes

A

catalytic proteins that speed up a reaction w/o being changed by it, by lowering the activation energy of the reaction

149
Q

define Free energy of activation (Ea)

A

energy required to begin a reaction

150
Q

Ea is often supplied in the form of….

A

thermal energy absorbed from the reactants’ surroundings

151
Q

define catalysis

A

lowering of the Ea barrier in order to speed up reactions

152
Q

define induced fit

A

brings chemical groups of the active site into positions that enhance their ability to catalyze the reaction

153
Q

define saturated enzyme

A

enzyme has all its active sites engaged

154
Q

If an enzyme is saturated, the reaction can only be sped up by…

A

adding more enzymes

155
Q

Why does each enzyme have optimal conditions for its functioning?

A

Optimal conditions favor the most active shape for an enzyme

156
Q

define competitite inhibitors

A

bind to the active sites of enzymes, competing with substrate

157
Q

define noncompetitive inhibitors

A

bind to another part of the enzyme, causing a conformational change that ↓ its activity

158
Q

define allosteric regulation

A

when a regulatory molecule binds to a protein one one site, causing a change in function at another site

159
Q

define activator (allosteric reg)

A

stabilizes the active form of the enzyme

160
Q

define inhibitor (allosteric reg)

A

stabilizes the inactive form of the enzyme

161
Q

define feedback inhibition

A

end product of a metabolic pathway shuts down the pathway

162
Q

feedback inhibition prevents…

A

waste of chemical resources

163
Q

define cofactors

A

inorganic “helpers” to enzymes - zinc, magnesium, iron, etc

164
Q

define coenzymes

A

organic cofactors - vitamins

165
Q

most allosterically regulated enzymes are made of…

A

polypeptide subunits, each with its own active site

166
Q

requirements for activators/inhibitors

A

only requires 1

167
Q

how does feedback inhibition work?

A

End product may bind to the first enzyme in a pathway, inactivating it

BI173—Cell & Organismal Biology (3 decks)

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