Fundamentals of Bio/Chemistry Flashcards

(219 cards)

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
glucose and fructose are _____ of each other
isomers
26
what type of carbohydrate results when 2 monosaccharides bond together?
disaccharide
27
_____ bring monosaccharides together
dehydration/condensation reactions
28
what reacts with what in a dehydration/condensation reaction?
hydroxyl (OH) + hydrogen (H)
29
what is formed and what is released in a condensation/ dehydration/condensation reaction?
covalent bond formation; release of H2O
30
what is the opposite of a condensation/dehydration reaction - why?
hydrolysis reaction; adds H2O to a covalent bond to split monomers apart
31
what is the name of the bond that occurs when a carbohydrate bonds to another molecule?
glycosidic
32
carbohydrates linked to lipids are known as _____
glycolipids
33
carbohydrates linked to proteins are known as _____
glycoproteins
34
the disaccharide _____ is table sugar
sucrose
35
which disaccharide contains 1 glucose and 1 fructose?
sucrose
36
which disaccharide contains 1 galactose and 1 glucose?
lactose
37
which disaccharide contains 2 glucoses?
maltose
38
polysaccharides are long polymers of _____
monosaccharides
39
_____ may or may not have branching
polysaccharides
40
some polysaccharides are for _____, and others are for structure.
storage
41
_____ is a crucial storage polysaccharide in plants
starch
42
starch contains many _____ monomers in linear forms as well as branched forms
glucose
43
linear plant starch is called _____
amylose
44
what type of glycosidic bonds are in amylose?
α-1,4-glycosidic bonds | linear
45
what is amylopectin?
branched form of plant starch
46
what type of glycosidic bonds are in amylopectin?
α-1,4-glycosidic (linear) α-1,6-glycosidic (branches)
47
_____ is a storage polysaccharide found in humans
glycogen
48
glycogen contains many _____ monomers
glucose
49
is amylopectin or glycogen more branched?
glycogen
50
what type of bonds does glycogen have?
α-1,4-glycosidic (linear) many α-1,6-glycosidic (branches)
51
which type of human tissues store glycogen?
liver (mostly); muscles
52
name two alpha-glucose polysaccharides
starch, glycogen
53
_____ is a structural polysaccharide in plant cell walls, wood, and paper
cellulose
54
cellulose is a _____ polymer
glucose
55
what type of bonds does cellulose contain - what do they do?
β-1,4-glycosidic; allow cellulose to linear strands that pack together in parallel
56
what type of intermolecular force holds adjacent cellulose strands together in parallel?
hydrogen bonds
57
cellulose's structure gives it a high _____
rigidity
58
can humans digest cellulose?
no - it passes through the digestive tract as fiber
59
chitin is a _____ polysaccharide
structural
60
chitin is found in _____ cell walls and _____ exoskeletons
fungal; insect
61
chitin is a structural polysaccharide of _____ monomers
N-acetylglucosamine
62
what type of bonds are in chitin?
β-1,4-glycosidic
63
chitin looks a lot like _____
cellulose | parallel strands cross-linked by H-bonds
64
name two beta-glucose polysaccharides
cellulose, chitin
65
proteins contain polymers called _____
polypeptides
66
polypeptides are polymers of _____ monomers
amino acid
67
in an amino acid, what 4 things is the central carbon bonded to?
H, NH2, COOH, R
68
how many amino acids are there?
20
69
amino acids in a polypeptide are linked by _____ covalent bonds
peptide
70
how do amino acids form peptide bonds with one another?
dehydration/condensation reactions
71
which type of reactions separate the amino acids of a polypeptide?
hydrolysis
72
a peptide bond is an _____ bond involving amino acids
amide
73
amide/peptide bonds occur between _____ and _____ functional groups
NH2; COOH
74
what enzymes catalyze peptide bond formation?
peptidyl transferases
75
peptidyl transferases are _____ transferases
aminoacyl
76
polypeptides have an _____ and _____ terminus
amino (N-); carboxyl (C-)
77
the _____ structure of a protein is its amino acid sequence
primary
78
all proteins have _____ structure
primary
79
the _____ structure of a protein is the 3D shape from intermolecular forces between the polypeptide backbone
secondary
80
the _____ is the amino acid structural features other than the R-group
polypeptide backbone
81
does secondary structure include interactions between R-group atoms?
no
82
which level of protein structure includes alpha helix and beta sheet?
secondary
83
what is the most common type of intermolecular force for secondary structure?
H-bonds
84
the _____ structure is the 3D structure due to non-covalent interactions between amino acid R-groups
tertiary
85
what are the common interactions between R-groups in tertiary structure?
ionic; hydrogen; dipole-dipole; van der Waal; hydrophobic; disulfide
86
what is the "covalent exception" in tertiary structure?
disulfide bonds | these are covalent
87
which amino acids allows disulfide bond formation?
cysteine
88
the _____ structure of a protein is the 3D structure from the grouping of two or more separate polypeptides
quaternary
89
while there are multiple polypeptide chains in quaternary structure, they function as _____
1 protein
90
what are 3 structural classifications of proteins?
fibrous; globular; intermediate
91
fibrous structural proteins are (soluble/insoluble)
insoluble
92
fibrous structural proteins are long polymer _____
fibers/sheets
93
_____ form the structural components of cells
fibrous structural proteins
94
what is an example of a fibrous structural protein?
collagen
95
globular structural proteins are (soluble/insoluble)
soluble
96
_____ structural proteins are folded tightly and perform many functions
globular
97
what is an example of a globular structural protein?
albumin
98
intermediate structural proteins are (soluble/insoluble)
soluble
99
_____ structural proteins are fiber-shaped and perform many functions
intermediate
100
what is an example of a intermediate structural protein?
fibrinogen
101
what are 2 compositional protein classifications?
simple; conjugated
102
simple protein compositions contain only _____
amino acids | ex: albumin
103
conjugated protein compositions contain _____
amino acids + non-protein components
104
what are some examples of conjugated proteins?
glycoproteins (mucin); metalloproteins (hemoglobin); lipoproteins (LDL/HDL)
105
_____ causes proteins to lose their secondary, tertiary, and quaternary structures
protein denaturation
106
denatured proteins retain their _____ structure
primary
107
loss of _____ leads to a loss of protein function
shape | denaturation
108
what are some causes of protein denaturation?
excess temperature, chemicals, pH changes, radiation
109
_____ are molecules that increase reaction rates
catalysts
110
despite speeding up reactions, catalysts do not affect the _____ of a reaction
spontaneity
111
_____ are not used up by the reactions they manipulate, meaning the reaction does not change them
catalysts
112
catalysts lower _____ to speed reactions
activation energies/transition state energies
113
_____ do not change energy absorbing reactions to energy releasing ones, or vice versa
catalysts
114
catalysts do not affect the energy of _____ or _____
reactants; products
115
_____ are biological, globular protein (usually) catalysts
enzymes
116
substrates bind to enzymes at the _____
active site
117
not all enzymes are proteins - give an example of an RNA enzyme:
ribozymes
118
active sites have unique properties and _____
substrate specificity
119
the _____ measures how efficient an enzyme is in converting substrate to product
specificity constant
120
enzymes bind at the active site via the _____ fit model
induced
121
non-protein molecules that assist enzymes
cofactors
122
cofactors usually help enzymes by donating/accepting some reaction component, like _____
electrons
123
what are organic cofactors (e.g. vitamins)?
coenzymes
124
inorganic cofactors are usually _____
metal ions
125
_____ refer to enzymes that are bound to their cofactor
holoenzymes
126
what is an apoenzyme?
an enzyme that is lacking (not bound to) its cofactor
127
cofactors that tightly/covalently bind to their enzyme are known as _____
prosthetic groups | forms a holoenzyme
128
enzyme efficiency is determined by _____ and _____
temperature; pH
129
_____ is a form of enzyme regulation, where inhibitors compete with substrates for active sites
competitive inhibition
130
we can outcompete a competitive inhibitor by adding more _____
substrate
131
what is enzyme saturation?
all active sites are occupied
132
_____ is when an inhibitor binds to the allosteric site
noncompetitive inhibition
133
what is an allosteric site?
a different location that is not the active site of enzyme catalysis
134
a noncompetitive inhibitor binding to the allosteric site modifies the _____ so that the substrate has reduced binding or cannot bind
active site
135
enzymes that have both an active site and an allosteric site
allosteric enzymes
136
a molecule that binds to an enzyme at a site other than the active site and affects its activity
allosteric effector
137
we cannot _____ allosteric inhibitors by adding more substrate
outcompete
138
the rate of enzyme catalysis is unaffected by increasing the substrate concentration in _____
noncompetitive inhibition
139
_____ is the substrate concentration at 50% of Vmax
Michaelis Constant (Km)
140
a _____ Km indicates that Vmax is reached at low substrate concentrations
small
141
a _____ Km indicates that Vmax is reached at high substrate concentrations
large
142
in competitive inhibition, Km is raised but Vmax _____
remains the same
143
in noncompetitive inhibition, Km stays the same but Vmax _____
is lowered
144
lipids are _____, non-polar molecules
hydrophobic
145
_____ store energy; insulation; cell membranes; endocrine
lipids
146
what are the components of a triglyceride?
three fatty acid chains attached to a glycerol backbone
147
what are adipocytes?
specialized fat cells that house triglycerides
148
triglycerides are produced by _____ reactions
dehydration/condensation
149
which groups of which molecules react to form a triglyceride?
glycerol (H)
150
what type of bonds exist between glycerol/fatty acids in a triglyceride?
ester
151
addition of H2O to a triglyceride's esters will break the fatty acids off the glycerol backbone by a _____ reaction
hydrolysis
152
_____ fatty acids have no double bonds
saturated
153
saturated fatty acids form _____, stacked chains
straight
154
saturated fatty acids tend to be _____ at room temperature
solid
155
_____ fatty acids can possess 1 (or more) double bonds
unsaturated
156
_____ fatty acids have 1 double bond
monounsaturated
157
polyunsaturated fatty acids have _____ double bonds
2 or more
158
cis-unsaturated fatty acids create _____ in the fatty acid chain, meaning they do not pack tightly
kinks
159
cis-unsaturated fats tend to be _____ at room temperature
liquid
160
trans-unsaturated fatty acids pack together _____, and they are very bad for health
tightly
161
_____ are a unique type of lipid (fat) in cell membranes
phospholipids
162
what are the components of a phospholipid?
2 fatty acids and 1 phosphate group attached to 1 glycerol backbone
163
phospholipids are _____, meaning they have both hydrophobic and hydrophilic properties
amphipathic
164
_____ are like phospholipids but with a carbohydrate group rather than a phosphate group
glycolipids
165
cell membranes form through _____ of phospholipids
self-assembly
166
_____ is another class of lipid that makes up around 30-50% of a eukaryotic cell membrane
cholesterol
167
cholesterol contains _____ hydrocarbon rings and is also amphipathic
four
168
what are the factors that modulate membrane fluidity?
temperature; cholesterol; degree of unsaturation in phospholipid fatty acid tails
169
what maintains membrane fluidity in the cold?
increasing phospholipid unsaturation; cholesterol
170
what maintains membrane fluidity in the heat?
decreasing phospholipid unsaturation; cholesterol
171
the _____ makes cholesterol, and we can also get it from the _____
liver; diet
172
cholesterol is a precursor to vitamin _____ and _____ acids
D; bile
173
_____ is a precursor to steroids
cholesterol
174
describe the general structure of a steroid:
fused 4 ring structure (3 cyclohexanes & 1 cyclopentane)
175
_____ are used as hormones and are a structural component of membranes (cholesterol)
steroids
176
lipids are insoluble and must be transported through the blood by _____
lipoproteins
177
lipoproteins contain a _____ of phospholipids, cholesterol, and proteins
coat
178
lipoproteins contain a _____ that contains more cholesterol and triglycerides
lipid core
179
_____ (lipoproteins) have a low density of proteins and are generally considered unhealthy
low-density lipoproteins (LDLs)
180
_____ (lipoproteins) have a high density of proteins and are generally considered to be healthy
high-density lipoproteins (HDLs)
181
waxes & carotenoids are _____ derivatives
lipid
182
esters of fatty acids and monohydroxy alcohols
waxes
183
waxes are used as a _____, protective coating
hydrophobic
184
carotenoid structure:
fatty acid carbon chains with conjugated double bounds and 6-membered rings at each end
185
carotenoid function:
pigments, which produce colors in plants and animals
186
what are 2 common nucleic acids to know?
DNA; RNA
187
_____ have a pentose sugar attached to a nitrogenous base
nucleosides
188
a _____ is a pentose sugar attached to a nitrogenous base and a single phosphate group
nucleotide
189
nucleic acids are polymers made of _____
nucleotides
190
nucleoside di- or triphosphates have more than 1 _____ group
phosphate
191
what are the 4 possible bases of a DNA nucleotide?
adenine, thymine, cytosine, guanine
192
what are the 4 possible bases of a RNA nucleotide?
adenine, uracil, cytosine, guanine
193
nucleotides can be further categorized depending on their nitrogen base as a _____ or _____
purine; pyrimidine
194
_____ bases have 2 rings
purine
195
_____ bases have 1 ring
pyrimidine
196
Adenine and Guanine have 2 rings and are classified as _____
PURines | PUR As Gold
197
Cytosine, Uracil, and Thymine have 1 ring and are classified as _____
pyrimidines | CUT the PY
198
_____ nucleotides have ribose sugars with a hydroxyl on the 2' carbon
RNA
199
_____ nucleotides have deoxyribose sugars without a hydroxyl on the 2' carbon
DNA
200
RNA is more reactive (less stable) than DNA because of its _____
2' hydroxyl
201
_____ groups attach to the nucleotide sugar at the 5' carbon
phosphate
202
5' _____ of one nucleotide connect to the 3' _____ of another nucleotide in nucleic acids
phosphates; hydroxyl
203
bonding between a 5' phosphate and a 3' hydroxyl creates a _____ bond in nucleic acids
phosphodiester
204
what creates the sugar-phosphate backbone of nucleic acid?
phosphodiester bonds
205
nucleic acids have _____, with a 5' and 3' end
directionality
206
_____ add to growing nucleic acid polymers by losing two phosphates (as _____)
nucleoside triphosphates; pyrophosphate
207
DNA manifests as a _____, _____ helix
antiparallel; double-stranded
208
purines can only H-bond to _____
pyrimidines
209
pyrimidines can only H-bond to _____
purines
210
adenine and thymine (or uracil) pair together via _____ hydrogen bonds
2
211
cytosine and guanine pair together via _____ hydrogen bonds
3
212
unlike DNA, RNA is usually _____ stranded
single
213
what are the 3 fundamental statements of the cell theory?
all lifeforms have 1 or more cells; cells are the most simple unit of life; cells come from other cells
214
does the cell-theory apply to viruses?
no - they are not living cells
215
the central dogma of genetics states that information flows from _____ to _____ to _____
DNA; RNA; proteins
216
an exception to the central dogma of genetics are _____, mis-folded proteins that cause other proteins to mis-fold
prions
217
what is the hypothesis for the creation of the first cell as we know it?
the RNA world hypothesis
218
the RNA world hypothesis suggests that self-replicating _____ molecules were the precursor to current life
RNA
219
what are 2 central facts that support the RNA world hypothesis?
RNA can: store genetic information like DNA; catalyze chemical reactions like proteins