Exam 1 Flashcards

1
Q

cell theory

A
  1. all organisms consist of one or more cells
  2. the cell is the basic unit of structure for all organisms
  3. all cells arise only from preexisting cells
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2
Q

focuses mainly on cellular structure and emphasizes optical techniques

A

cytology

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3
Q

focuses mainly on cellular function

A

biochemistry

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4
Q

focuses on info flow and heredity

A

genetics

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5
Q
  • earliest tool of cytologists

- allowed for identification of organelles within cells

A

light microscope

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6
Q

white light is passed through a specimen and the background is illuminated
high contrast
stained specimens

A

bright-field microscopy

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7
Q

improves contrast without staining or sectioning

living cells

A

phase contrast microscopy

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8
Q

gives strong signal at edges

3D

A

DIC/normarski

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9
Q

fluorescent molecules used to label cellular components

A

fluorescence microscopy

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10
Q

a type of fluorescent microscopy that controls the plane in which the data is collected

A

confocal microscopy

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11
Q

uses a beam of electrons that is deflected and focused by an electromagnetic field
much better resolution and higher magnification

A

electron microscope

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12
Q

the surface of a specimen is scanned by utilizing electrons that have bounced off

A

scanning electron microscopy

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13
Q

forms images from electrons that are transmitted through a specimen

A

transmission electron microscopy

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14
Q

the ability to enlarge something in appearance

A

magnification

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15
Q

the ability to see two neighboring points in the visual field as distinct entities

A

resolution

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16
Q

trace the fate of specific atoms and molecules

A

radioactive isotopes

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17
Q

separate different structures and macromolecules based on shape, size or density

A

subcellular fractionation

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18
Q

techniques to separate molecules from a solution based on size, charge or chemical affinity

A

chromotography

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19
Q

uses electrical field to separate molecules based on their mobility

A

electrophoresis

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20
Q

to determine the size and composition of individual proteins

A

mass spectometry

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21
Q

hereditary factors

A

genes

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22
Q

threadlike bodies in the nucleus; carries genetic material

A

chromosomes

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23
Q

hereditary factors are located on the chromosomes in the nucleus

A

chromosome theory of hereditary

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24
Q

a variety of techniques that use the ability of nucleic acid bases to bind to each other

A

nucleic acid hybridization

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25
restriction enzymes cut DNA at specific places allowing scientists to create recombinant DNA molecules
recombinant DNA technology
26
methods for rapidly determining the base sequences of DNA molecules
DNA sequencing
27
merges computer science with biology to organize and interpret enormous amounts of sequencing and other data
bioinformatics
28
allows determination of how proteins interact within a cell
yeast two-hybrid system
29
development of tiny tools, sensors, and computer-aided analysis of the results
nanotechnology
30
statement consistent with most of the data, may take the form of a model; must be testable
hypothesis
31
a hypothesis that has been expansively tested; widely accepted
theory
32
a theory that has been tested and confirmed
law
33
using purified chemicals and cellular components
in vitro
34
using live cells or organisms
in vivo
35
using computer analysis of large amounts of data
in silico
36
species that is widely studied, well characterized, easy to manipulate, and is useful for experimental studies
model organism
37
elements of water are lost, simple compounds form a stable polymer
condensation
38
splitting by adding the elements of water
hydrolysis
39
number of carbons in an atom's outer orbital
valence
40
the sharing of a pair of electrons between two atoms
covalent bonds
41
the amount of energy required to break 1 mole of bonds; expression of stability
bond energy
42
electrons are not shared equally between two atoms; shared electrons stay closest to the nucleus with the highest electronegativity
polar bonds
43
molecules with asymmetric distribution of charge
polar molecules
44
molecules that lack polarized bonds
nonpolar molecules
45
results when strongly EN nuclei capture electrons
ions
46
have extra electrons; negatively charged
anion
47
have lost electrons; positively charged
cation
48
unstable atoms or molecules with unpaired electrons
free radicals
49
mirror image of the same compound
stereoisomer
50
atom with four differs substituents
asymetric carbon
51
an extensive network of hydrogen bonds
cohesive
52
4 main properties of hydrogen bonds/water
surface tension high boiling point high specific heat high heat of vaporization
53
the amount of heat a substance must absorb to raise its temp 1*C
specific heat
54
the amount of energy required to convert one gram of liquid to vapor
heat of vaporization
55
fluid in which another substance can dissolve
solvent
56
regions of polar and non-polar molecules
amphipathic
57
readily permeable to nonpolar molecules but impermeable to most polar molecules and ions
selectively permeable
58
biological molecules and structures are organized into a series of levels each building on the preceding one
cellular heirarchy
59
components of organelles and other sub cellular structures that make up the cell
supramolecular structures
60
the macromolecules that are responsible for most of the form and order of living systems are generated by polymerization of small organic molecules
the fundamental principle of biological chemistry
61
information needed to specific the folding of macromolecules and their interaction to form complex structures is inherent in the polymers themselves
principle of self-assembly
62
complex of nucleic acid and proteins
virus
63
dependence on subassemblies that act as intermediates of the process of assembly of increasingly complex structures
hierarchical assembly
64
relatively few subunits are used for a wide variety of structures
chemical simplicity | advantage of hierarchical assembly
65
a small number of kinds of condensation reactions are needed
efficiency of assembly | advantage of hierarchical assembly
66
defective components can be discarded prior to incorporation into higher-level structure that is more costly to replace. reducing the waste of energy and materials
quality control | advantage of hierarchical assembly
67
large structural and functional molecules in cells
macromolecules
68
macromolecules used for enzymes, structure, motility, regulation, transport, communication, defense, storage
proteins
69
amino acid links
peptide bonds
70
process of elongating a chain of amino acids
protein synthesis: translation
71
a single polypeptide
monomeric proteins
72
two+ polypeptides
multimeric proteins
73
sulfur bonds between two cysteine
disulfide bridges
74
amino acid sequence
primary structure
75
local regions of structure hydrogen bonding between NH and CO groups a helix and b sheet
secondary structure
76
depends on long distance interaction between R groups
tertiary structure
77
the most stable possible 3D structure of a particular polypeptide
native conformation
78
have extensive regions of secondary structure, giving a highly ordered, repetitive structure
fibrous protein
79
discrete locally folded unit of tertiary structure usually with a specific function
domain
80
the level of organization concerned with subunit interactions and assembly
quarternary structure
81
a higher level of assembly in the case of proteins (often enzymes)
multiprotein complexes
82
store, transmit and express genetic information
nucleic acid
83
the sugar-based portion without the phosphate group
nucleoside
84
nucleosides with one phosphate group
nucleoside monophosphates
85
polymers of sugars and sugar derivatives that are not informational molecules
polysaccharides
86
short polymers sometimes attached to cell surface proteins
oligosaccharides
87
depiction of the linear molecule
Fischer projection
88
shows the ring form of the molecule
Haworth projection
89
two monosaccharide units are covalently linked
disaccharides
90
liking of disaccharides | -C-O-C-
glycosidic bond
91
highly branched | stored in liver
glycogen
92
glucose reserve in plants amylose (unbranched) amylopectin (branched)
starch
93
found in plant cell walls composed of repeating monomers of Beta D-glucose
cellulose
94
component of invertebrate exoskeleton
Chitin
95
composed of two different sugars found in extracellular space
GAGs
96
each carbon atom in the chain is bonded to the max number of hydrogens
saturated fatty acids
97
have one or more doubly bonds so have bends in the chains and less tight packing
unsaturated fatty acids
98
a type of unsaturated fatty acid with a particular type of double bond that causes less of a bend in the chain
trans fats
99
glycerol molecule with three fatty acids; main function is energy storage
trigylcerols
100
are important to membrane structure due to their ampipathic nature
phospholipids
101
lipids containing a carbohydrate instead of a phosphate group
glycolipids
102
derivatives of a four-ringed hydrocarbon skeleton which distinguishes them from other lipids
steroids
103
most common steroid in animal cells; also the starting material for synthesis of steroid hormones
cholesterol
104
synthesized from the 5-carbon compound isoprene
terpenes
105
most of the commonly encountered single-celeld, non-nucleated organisms
bacteria
106
species that live in extreme habits and have diverse metabolic strategies
archaea
107
need for adequate SA:V ration rates at which molecules can diffuse need to maintain adequate local concentrations of substances required for necessary cellular functions
limits to cell size
108
unassisted movement of a substance from a region of high concentration to a region of low concentration
diffusion
109
membrane bounded compartments that are specialized for specific functions
organelles
110
genetic information of a bacterial or archaeal cell folded into a compact structure
nucleoid
111
suggests that mitochondria and chloroplasts originated from prokaryotes
endosymbiont theory
112
plant cells are connected to neighboring cells by cytoplasm bridges
plasmodesmata
113
animal cells communicate with one another through intercellular connections
gap junctions | also tight junctions adhesion junctions
114
noncellular parasitic particles incapable of a free living existence; consist of nucleic acid and protein; invade and infect cells
viruses
115
simpler than viruses; small circular RNA molecules, the smallest known infectious agents
viroids
116
proteinaceous infective particles that are responsible for neurological diseases; abnormally folded versions of normal cellular proteins
prions
117
capacity to cause specific chemical or physical change
energy
118
formation of new chemical bonds and the synthesis of new molecules; required for growth and maintenance of cells and cellular structures
biosynthesis
119
physical change in the position or orientation of a cell or some part of it
mechanical work
120
moving molecules across a membrane against a concentration gradient
concentration work
121
ions are transported across a membrane against an electrochemical gradient
electrical work
122
the production of light;
bioluminescence
123
capture light energy form the sun and transform it into chemical energy stored as ATP
phototrophs
124
use solar energy to produce all the carbon compounds they need from CO2
photoautotrophs
125
harvest solar energy for some cellular activities but rely on intake of organic molecules as a source of carbon
photoheterotrophs
126
obtain energy by oxidizing chemical bonds in molecules
chemotrophs
127
oxidize inorganic compounds or inorganic ions for energy, and use CO2 as a carbon source
chemoautotrophs
128
ingest and use chemical compounds to provide both energy and carbon for cellular needs
chemoheterotrophs
129
removal of electrons from a substance, usually hydrogen atoms
oxidation
130
addition of electrons to a substance through addition of hydrogen atoms
reduction
131
study of changes in energy that accompany events in the universe
thermodynamics
132
applies principles of thermodynamics to the biological world
bioenergetics
133
restricted portion of the universe that is being considered
system
134
the rest of the universe
surroundings
135
sealed from is environment and cannot take in nor release energy
closed system
136
can have energy added to it or removed from it
open system
137
each of its variable properties is held at a specified value
state
138
the use of energy to drive a process other than heat flow
work
139
the amount of energy required to raise one gram of water by one degree centigrade at one atmosphere of pressure
calorie
140
law of conservation of energy in every physical or chemical change the total amount of energy in the universe remains constant energy cannont be created or destroyed
first law of thermodynamics
141
total energy stored within a system
internal energy
142
heat content is exalted to E, dependent on pressure and volume
enthaply
143
energy is released; deltaH is negative
exothermic
144
energy is absorbed; deltaH is positive
endothermic
145
a favorable reaction and can occur without the input of external energy
thermodynamically spontaneous reaction
146
a measure of whether of not a reaction or process can occur
thermodynamic spontaneity
147
in every physical or chemical change the universe tends toward greater disorder or randomness; allows us to predict what direction a reaction will proceed under specific conditions, how much energy will be released, and how changes in conditions will affect is
second law of thermodynamics
148
randomness or disorder
entropy
149
measure of spontaneity for a system alone; readily measurable indicator of spontaneity
free energy
150
reactions are energy-yielding and occur spontaneously
exergonic
151
reactions are energy-requiring and do not occur spontaneously under the conditions specified
endergonic
152
a reaction can take place, not that it will; usually an input of activation energy is required
spontaneous
153
measure of directionality
equilibrium constant
154
25C 1 atm 1M pH 7
standard state
155
refers to conversion of a mol of reactant to products under conditions where, temp, pressure, pH and concentrations of all are maintained at their standard values
standard free energy change
156
concentrations of reactants and products remain relatively constant, but not at equilibrim
steady state
157
all cellular processes or reactions are mediated by protein catalysts
enzyme catalysis
158
the minimum amount of energy required before collisions between the reactants will give rise to products
activation energy
159
intermediate chemical stage which has a free energy higher than that of the initial reactants
transition state
160
molecules that are thermodynamically unstable but do not have enough energy to exceed the activation energy barrier
metastable state
161
enhances the rate of a reaction by providing such a surface and lowering Ea
catalyst
162
three properties of catalysts
increase reaction rate by lowering the Ea required form transient, reversible complexes with substrate molecules change the rate which equilibrium is achieved
163
a characteristic cluster of amino acids
active site
164
inorganic enzyme conjugates
cofactors
165
organic enzyme conjugates
coenzymes
166
ability to discriminate between very similar molecules
substrate specificity
167
enzymes accept any of an entire group substrates sharing a common feature
group specificity
168
enzyme holds substrate in the optimal position for reaction
substrate orientation
169
substrate binding at the active site induces a conformational change in the shape of the enzyme
induced-fit model
170
the study of rate of enzymatic factions under various experimental conditions
enzyme kinetics
171
measured over a brief time during which the substrate concentration has not yet decreases enough to affect the rate of reaction
initial reaction rate
172
rate of change in product concentration per unit time
initial reaction velocity
173
as [S] tends toward infinity, v. approaches an upper limiting value
maximum velocity
174
inability of increasingly higher substate concentrations to increase the faction velocity beyond a finite upper value
saturation
175
the concentration of substrate that gives half maximum velocity
Km
176
rate at which substrate molecules are converted to product by a single enzyme at maximum velocity
turnover number Kcat
177
compounds that resemble real substrates or transition states closely enough to occupy the active site but not closely enough to complete the reaction
substrate analogs and transition state analogs
178
bind the enzyme covalently and cause permanent loss of catalytic activity
irreversible inhibitors
179
bind enzymes noncovalently and can dissociate from the enzyme
reversible inhibitors
180
bind the active site of an enzyme and compete with substrate for the active site
competitive inhibitors
181
bind the enzyme at a location other than the active site and inhibit directly; cause conformation change in the enzyme that either inhibits substrate binding at the active site OR reduces catalytic activity at the active site
noncompetitive inhibition
182
depends on interactions of substrates and products with an enzyme
substrate-level regulation
183
the single most important control mechanism whereby the rates of enzymatic reactions are adjusted to meet the cell's needs
allosteric regulation
184
have two conformations one in which it has affinity for the substrate and one in which it does not
allosteric enzymes
185
makes use of this property by regulating the conformation of the enzyme
allosteric regulation
186
regulates enzyme activity by binding and stabilizing one of the conformations
allosteric effector
187
allosteric effector binds a site distinct from the active site
allosteric (or regulatory) site
188
active and allosteric sites are on different subunits
catalytic and regulatory subunites
189
conformation change increases affinity for substrate
positive cooperativity
190
affinity for substrate is decreased
negative cooperativity
191
final product of an enzyme pathway negatively regulates an earlier step in the pathway
feedback inhibition
192
enzymes are subject to this | activity is regulated by addition or removal of groups, such as phosphate, methyl, acetyl groups etc.
covalent modification
193
reversible addition of phosphate groups
phosphorylation
194
catalyze the phosphorylation of other proteins
protein kinases
195
removal of phosphate groups from proteins
dephosphorylation
196
catalyze the dephosphorylation of other proteins
protein phosphatases
197
activation of a protein by a one-timid irreversible removal of part of the polypeptide chain
proteolytic cleavage
198
RNA molecules that have catalytic activity
ribozymes