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
elements that comprise 96% of living matter
carbon hydrogen oxygen nitrogen
26
4 major properties of water
1. cohesive behavior 2. ability to moderate temperature (high specific heat) 3. expansion upon freezing 4. versatility as a solvent
27
why is cohesive behavior important in water?
allows water to flow against gravity in plants
28
define specific heat
amt of heat that must be absorbed/lost for 1 g of a substance to change temp by 1 degree C
29
2 properties of water that help organisms maintain stable temp
high specific heat evaporative cooling
30
water reaches greatest density at ___ degrees C
4
31
if ice sank…
all bodies of water would eventually freeze
32
define hydration shell
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)
33
explain dissociation of water
loses H+ — becomes OH- (hydroxide) gains H+ — becomes H3O+ (hydronium)
34
\_\_\_\_\_\_ protect organisms from extremes of pH
buffers
35
most biological fluids are between \_\_\_-\_\_\_ pH
6-8
36
study of compounds containing carbon
organic chemistry
37
_structure of carbon_ protons valence electrons
6 4
38
In molecules w/ multiple carbons, each carbon bonded for 4 other atoms has a _______ shape
tetrahedral
39
In molecules w/ 2 atoms joined by a double bond, the atoms joined are __________ as the carbon
in the same plane
40
define hydrocarbons
organic molecules only consisting of C and H
41
\_\_\_\_\_\_\_\_ undergo reactions to release large amounts of energy
hydrocarbons
42
same molecular formula, but different structure & properties
isomers
43
3 types of isomers
structural geometric/cis-trans enantiomers
44
what are structural isomers?
different covalent arrangements - different shape
45
what are geometric isomers? what do cis and trans mean?
* same covalent bonds, but different structural arrangement * Cis - “x” atoms on same side * Trans - “x” atoms on opposite sides
46
what are enantiomers?
isomers that are mirror images of one another
47
examples of enantiomers
S ibuprofen works, R ibuprofen does not R albuterol works, S albuterol does not
48
components of organic molecules most involved in chemical reactions
functional groups
49
define polymers
long chains of monomers
50
macromolecules are made of…
polymers
51
only non-macromolecule biomolecule
lipids
52
explain synthesis of polymers
* _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
53
explain breakdown of polymers
* _Hydrolysis_ - disassembly of polymers with addition of water - reverse of dehydration reaction
54
lipids consist mainly of…
hydrocarbons
55
most biologically important lipids
fats phospholipids steroids
56
components of fats
glycerol fatty acids
57
what is a glycerol?
3-carbon alcohol with hydroxyl group attached to each carbon
58
what is a fatty acid?
carboxyl group attached to long carbon skeleton
59
explain saturated fatty acids shape? state? source?
every available area on C is linked to H (all single bonds) straight shape solid at room temp most animal fats
60
explain unsaturated fatty acids shape? state? source?
have 1+ double bonds between C - prevent saturation with H bent shape liquid at room temp (“oils”) most plant and fish fats
61
major functions of fats
energy storage cushioning insulation
62
components of phospholipids
2 fatty acids & a phosphate group attached to a glycerol
63
natural arrangement of phospholipids
bilayer
64
components of steroids
Lipids with carbon skeleton consisting of 4 fused rings
65
functions of cholesterol
component of animal cell membranes & precursor from which all other steroids are synthesized
66
covalent bond unique to lipids connects glycerol to fatty acids
ester linkage
67
most basic formula of monosaccharides
CH2O
68
monosaccharides classified by…
location of carbonyl group & number of carbons in skeleton
69
Glucose + glucose =
maltose
70
glucose + fructose =
sucrose
71
covalent bond between monosaccharides
glycosidic linkage
72
storage polysaccharide in plants
starch
73
starch is stored as…
granules in chloroplasts & other plastids
74
simplest starch
amylose
75
animal storage of polysaccharides
glycogen
76
major component of tough wall of plant cells
cellulose
77
how is cellulose structured differently from starch?
OH side of the glucose is flipped on every other one
78
where is chitin found?
exoskeleton of arthropods (embedded in proteins) cell walls of fungi
79
in aqueous solutions, most sugars form…
rings
80
function of nucleic acids
Store, transmit & help express genetic information
81
monomers of nucleic acids
nucleotides
82
functions of DNA
includes directions for its own replication directs synthesis of mRNA controls protein synthesis (gene expression)
83
function of mRNA
interacts with ribosomes to direct production of a polypeptide
84
polymers of nucleic acids
polynucleotides
85
components of nucleotides
a nitrogenous base, a pentose sugar, and 1+ phosphate groups
86
what is a nucleoside?
portion of a nucleotide w/o the phosphate
87
pentose sugar in DNA & RNA
dna - deoxyribose rna - ribose
88
2 families of nucleotides & their structures
* _Pyrimidines_ - cytosine, thymine, uracil - single 6-membered ring (smaller) * _Purines_ - adenine, guanine - 6-membered ring fused to a 5-membered ring (larger)
89
linkages of nucleic acids
phosphodiester bonds
90
sugar-phosphate forms the _______ of DNA while the nitrogenous bases are \_\_\_\_\_\_\_\_
backbone appendages
91
codon
3 bases coding for 1 amino acid
92
which directions are genes read in?
5 prime to 3 prime
93
basic structure of DNA
_Double helix_ - 2 polynucleotides spiraling around an imaginary axis - backbones run in opposite directions (_antiparallel_)
94
\_\_ hydrogen bonds between A & T \_\_ hydrogen bonds between C & G
2 3
95
define protein
biologically functional molecule consisting of 1+ polypeptides
96
define polypeptide
unbranched polymers built from amino acids
97
2 ends of a polypeptide
carboxyl end (_c-terminus_) amino end (_n-terminus_)
98
structure of an amino acid
amino and carboxyl groups bound by an alpha carbon unique R group
99
bonds used in proteins
peptide bonds
100
proteins account for \>\_\_% of dry mass of cells
50
101
major functions of proteins (8)
* 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
what is primary structure?
unique sequence of amino acids - determined by genetic info
103
what is secondary structure?
coils (helices) & folds (pleated sheets) in polypeptide chain
104
what is tertiary structure?
overall shape, resulting from interactions among various side chains (R groups) rather than backbone constituents
105
what is quaternary structure?
when a protein consists of multiple polypeptide chains folded together (does not occur in all proteins)
106
what allows hydrogen bonding in polypeptides?
Backbone of the chains have O bound to C (-) and H bound to O (+) at different spots
107
hydrogen bonding between repeating constituents of the polypeptide backbone
secondary structure
108
interactions among various side chains (R groups)
tertiary structure
109
tertiary structure includes which types of bonds?
hydrogen bonds ionic bonds hydrophobic interactions (cluster on the inside of the protein) van der waals interactions
110
strong covalent bonds that reinforce protein’s structure
disulfide bridges
111
fibrous protein consisting of 3 polypeptides coiled like rope
collagen
112
hemoglobin consists of…
4 polypeptides (2 alpha and 2 beta subunits)
113
begins with a specific molecule (substrate) & ends with a product
metabolic pathway
114
energy is released by breaking down complex molecules
catabolic pathway
115
consumes energy in order to build complex molecules from simpler ones
anabolic pathway
116
study of how energy flows through living organisms
bioenergetics
117
define energy
capacity to cause change
118
define thermal energy
kinetic energy associated with random movement of atoms/molecules
119
define heat
thermal energy transfer between objects
120
define potential energy
energy that matter possesses because of its location or structure
121
define chemical energy
potential energy available for release in a chemical reaction
122
study of energy transformation
thermodynamics
123
energy of the universe is constant
1st law of TD
124
During every transfer of energy, some energy is unusable and “lost” as \_\_\_\_\_\_
thermal energy
125
every transfer of energy increases the entropy of the universe
2nd law of TD
126
define entropy
measure of randomness/molecular disorder measure of thermal energy not available to use in work
127
examples of entropy increasing
increases as water boils as salt dissolves in water as we digest complex molecules
128
define spontaneous processes
occur w/o energy input energetically favorable
129
example of a spontaneous process
water running down a hill
130
processes that decrease entropy are \_\_\_\_\_\_\_\_\_; occur only if energy is provided
nonspontanteous
131
why don't organisms violate 2nd law?
Entropy may decrease in a particular system, as long as the total entropy of the system’s surroundings (universe) increases
132
\_\_\_\_\_\_\_\_\_\_\_\_\_\_\_\_ of a reaction tells us whether or not the reaction occurs spontaneously
Free-energy change (ΔG)
133
energy that can do work measure of a system’s instability tendency to change to a more stable state
Gibbs free energy
134
ΔG =
ΔH - TΔS
135
​​ΔG is ________ for all spontaneous processes 0 or ______ ΔG requires energy
negative for spontaneous processes 0 or positive requires energy
136
define equilibrium
state of maximum stability
137
only an ______ system can reach equilibrium
isolated
138
define exergonic reactions
spontaneous becomes more stable net release of free energy
139
define endergonic reactions
nonspontaneous becomes less stable absorbs free energy from its surroundings
140
composition of ATP
ribose (sugar) adenine (nitrogenous base) 3 phosphate groups
141
define phosphorylation
the 3rd phosphate is transferred to another molecule (the _phosphorylated intermediate_)
142
ATP powers cellular work by…
_coupling_ exergonic reactions with endergonic reactions
143
overall, coupled reactions are…
exergonic (ΔG is negative)
144
exergonic = (-/+) ΔG
negative
145
endergonic = (-/+) ΔG
positive
146
3 main kinds of cellular work
* Chemical - pushing endergonic reactions * Transport - pushing substances against direction of spontaneous movement (gradient) * Mechanical - ex contraction of muscle cells
147
Energy to phosphorylate ADP comes from…
catabolic reactions in the cell
148
define enzymes
catalytic proteins that speed up a reaction w/o being changed by it, by lowering the activation energy of the reaction
149
define Free energy of activation (Ea)
energy required to begin a reaction
150
Ea is often supplied in the form of….
thermal energy absorbed from the reactants’ surroundings
151
define catalysis
lowering of the Ea barrier in order to speed up reactions
152
define induced fit
brings chemical groups of the active site into positions that enhance their ability to catalyze the reaction
153
define saturated enzyme
enzyme has all its active sites engaged
154
If an enzyme is saturated, the reaction can only be sped up by…
adding more enzymes
155
Why does each enzyme have optimal conditions for its functioning?
Optimal conditions favor the most active shape for an enzyme
156
define competitite inhibitors
bind to the active sites of enzymes, competing with substrate
157
define noncompetitive inhibitors
bind to another part of the enzyme, causing a conformational change that ↓ its activity
158
define allosteric regulation
when a regulatory molecule binds to a protein one one site, causing a change in function at another site
159
define activator (allosteric reg)
stabilizes the active form of the enzyme
160
define inhibitor (allosteric reg)
stabilizes the inactive form of the enzyme
161
define feedback inhibition
end product of a metabolic pathway shuts down the pathway
162
feedback inhibition prevents…
waste of chemical resources
163
define cofactors
inorganic “helpers” to enzymes - zinc, magnesium, iron, etc
164
define coenzymes
organic cofactors - vitamins
165
most allosterically regulated enzymes are made of…
polypeptide subunits, each with its own active site
166
requirements for activators/inhibitors
only requires 1
167
how does feedback inhibition work?
End product may bind to the first enzyme in a pathway, inactivating it