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Cell Molec > Exam 1 > Flashcards

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
Q

restriction enzymes cut DNA at specific places allowing scientists to create recombinant DNA molecules

A

recombinant DNA technology

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26
Q

methods for rapidly determining the base sequences of DNA molecules

A

DNA sequencing

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27
Q

merges computer science with biology to organize and interpret enormous amounts of sequencing and other data

A

bioinformatics

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28
Q

allows determination of how proteins interact within a cell

A

yeast two-hybrid system

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29
Q

development of tiny tools, sensors, and computer-aided analysis of the results

A

nanotechnology

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30
Q

statement consistent with most of the data, may take the form of a model; must be testable

A

hypothesis

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31
Q

a hypothesis that has been expansively tested; widely accepted

A

theory

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32
Q

a theory that has been tested and confirmed

A

law

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33
Q

using purified chemicals and cellular components

A

in vitro

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34
Q

using live cells or organisms

A

in vivo

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35
Q

using computer analysis of large amounts of data

A

in silico

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36
Q

species that is widely studied, well characterized, easy to manipulate, and is useful for experimental studies

A

model organism

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37
Q

elements of water are lost, simple compounds form a stable polymer

A

condensation

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38
Q

splitting by adding the elements of water

A

hydrolysis

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39
Q

number of carbons in an atom’s outer orbital

A

valence

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40
Q

the sharing of a pair of electrons between two atoms

A

covalent bonds

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41
Q

the amount of energy required to break 1 mole of bonds; expression of stability

A

bond energy

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42
Q

electrons are not shared equally between two atoms; shared electrons stay closest to the nucleus with the highest electronegativity

A

polar bonds

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43
Q

molecules with asymmetric distribution of charge

A

polar molecules

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44
Q

molecules that lack polarized bonds

A

nonpolar molecules

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45
Q

results when strongly EN nuclei capture electrons

A

ions

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46
Q

have extra electrons; negatively charged

A

anion

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47
Q

have lost electrons; positively charged

A

cation

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48
Q

unstable atoms or molecules with unpaired electrons

A

free radicals

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49
Q

mirror image of the same compound

A

stereoisomer

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50
Q

atom with four differs substituents

A

asymetric carbon

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51
Q

an extensive network of hydrogen bonds

A

cohesive

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52
Q

4 main properties of hydrogen bonds/water

A

surface tension
high boiling point
high specific heat
high heat of vaporization

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53
Q

the amount of heat a substance must absorb to raise its temp 1*C

A

specific heat

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54
Q

the amount of energy required to convert one gram of liquid to vapor

A

heat of vaporization

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55
Q

fluid in which another substance can dissolve

A

solvent

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56
Q

regions of polar and non-polar molecules

A

amphipathic

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57
Q

readily permeable to nonpolar molecules but impermeable to most polar molecules and ions

A

selectively permeable

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58
Q

biological molecules and structures are organized into a series of levels each building on the preceding one

A

cellular heirarchy

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59
Q

components of organelles and other sub cellular structures that make up the cell

A

supramolecular structures

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60
Q

the macromolecules that are responsible for most of the form and order of living systems are generated by polymerization of small organic molecules

A

the fundamental principle of biological chemistry

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61
Q

information needed to specific the folding of macromolecules and their interaction to form complex structures is inherent in the polymers themselves

A

principle of self-assembly

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62
Q

complex of nucleic acid and proteins

A

virus

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63
Q

dependence on subassemblies that act as intermediates of the process of assembly of increasingly complex structures

A

hierarchical assembly

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64
Q

relatively few subunits are used for a wide variety of structures

A

chemical simplicity

advantage of hierarchical assembly

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65
Q

a small number of kinds of condensation reactions are needed

A

efficiency of assembly

advantage of hierarchical assembly

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66
Q

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

A

quality control

advantage of hierarchical assembly

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67
Q

large structural and functional molecules in cells

A

macromolecules

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68
Q

macromolecules used for enzymes, structure, motility, regulation, transport, communication, defense, storage

A

proteins

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69
Q

amino acid links

A

peptide bonds

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70
Q

process of elongating a chain of amino acids

A

protein synthesis: translation

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71
Q

a single polypeptide

A

monomeric proteins

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72
Q

two+ polypeptides

A

multimeric proteins

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73
Q

sulfur bonds between two cysteine

A

disulfide bridges

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74
Q

amino acid sequence

A

primary structure

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75
Q

local regions of structure
hydrogen bonding between NH and CO groups
a helix and b sheet

A

secondary structure

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76
Q

depends on long distance interaction between R groups

A

tertiary structure

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77
Q

the most stable possible 3D structure of a particular polypeptide

A

native conformation

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78
Q

have extensive regions of secondary structure, giving a highly ordered, repetitive structure

A

fibrous protein

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79
Q

discrete locally folded unit of tertiary structure usually with a specific function

A

domain

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80
Q

the level of organization concerned with subunit interactions and assembly

A

quarternary structure

81
Q

a higher level of assembly in the case of proteins (often enzymes)

A

multiprotein complexes

82
Q

store, transmit and express genetic information

A

nucleic acid

83
Q

the sugar-based portion without the phosphate group

A

nucleoside

84
Q

nucleosides with one phosphate group

A

nucleoside monophosphates

85
Q

polymers of sugars and sugar derivatives that are not informational molecules

A

polysaccharides

86
Q

short polymers sometimes attached to cell surface proteins

A

oligosaccharides

87
Q

depiction of the linear molecule

A

Fischer projection

88
Q

shows the ring form of the molecule

A

Haworth projection

89
Q

two monosaccharide units are covalently linked

A

disaccharides

90
Q

liking of disaccharides

-C-O-C-

A

glycosidic bond

91
Q

highly branched

stored in liver

A

glycogen

92
Q

glucose reserve in plants
amylose (unbranched)
amylopectin (branched)

A

starch

93
Q

found in plant cell walls composed of repeating monomers of Beta D-glucose

A

cellulose

94
Q

component of invertebrate exoskeleton

A

Chitin

95
Q

composed of two different sugars found in extracellular space

A

GAGs

96
Q

each carbon atom in the chain is bonded to the max number of hydrogens

A

saturated fatty acids

97
Q

have one or more doubly bonds so have bends in the chains and less tight packing

A

unsaturated fatty acids

98
Q

a type of unsaturated fatty acid with a particular type of double bond that causes less of a bend in the chain

A

trans fats

99
Q

glycerol molecule with three fatty acids; main function is energy storage

A

trigylcerols

100
Q

are important to membrane structure due to their ampipathic nature

A

phospholipids

101
Q

lipids containing a carbohydrate instead of a phosphate group

A

glycolipids

102
Q

derivatives of a four-ringed hydrocarbon skeleton which distinguishes them from other lipids

A

steroids

103
Q

most common steroid in animal cells; also the starting material for synthesis of steroid hormones

A

cholesterol

104
Q

synthesized from the 5-carbon compound isoprene

A

terpenes

105
Q

most of the commonly encountered single-celeld, non-nucleated organisms

A

bacteria

106
Q

species that live in extreme habits and have diverse metabolic strategies

A

archaea

107
Q

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

A

limits to cell size

108
Q

unassisted movement of a substance from a region of high concentration to a region of low concentration

A

diffusion

109
Q

membrane bounded compartments that are specialized for specific functions

A

organelles

110
Q

genetic information of a bacterial or archaeal cell folded into a compact structure

A

nucleoid

111
Q

suggests that mitochondria and chloroplasts originated from prokaryotes

A

endosymbiont theory

112
Q

plant cells are connected to neighboring cells by cytoplasm bridges

A

plasmodesmata

113
Q

animal cells communicate with one another through intercellular connections

A

gap junctions

also tight junctions adhesion junctions

114
Q

noncellular parasitic particles incapable of a free living existence; consist of nucleic acid and protein; invade and infect cells

A

viruses

115
Q

simpler than viruses; small circular RNA molecules, the smallest known infectious agents

A

viroids

116
Q

proteinaceous infective particles that are responsible for neurological diseases; abnormally folded versions of normal cellular proteins

A

prions

117
Q

capacity to cause specific chemical or physical change

A

energy

118
Q

formation of new chemical bonds and the synthesis of new molecules; required for growth and maintenance of cells and cellular structures

A

biosynthesis

119
Q

physical change in the position or orientation of a cell or some part of it

A

mechanical work

120
Q

moving molecules across a membrane against a concentration gradient

A

concentration work

121
Q

ions are transported across a membrane against an electrochemical gradient

A

electrical work

122
Q

the production of light;

A

bioluminescence

123
Q

capture light energy form the sun and transform it into chemical energy stored as ATP

A

phototrophs

124
Q

use solar energy to produce all the carbon compounds they need from CO2

A

photoautotrophs

125
Q

harvest solar energy for some cellular activities but rely on intake of organic molecules as a source of carbon

A

photoheterotrophs

126
Q

obtain energy by oxidizing chemical bonds in molecules

A

chemotrophs

127
Q

oxidize inorganic compounds or inorganic ions for energy, and use CO2 as a carbon source

A

chemoautotrophs

128
Q

ingest and use chemical compounds to provide both energy and carbon for cellular needs

A

chemoheterotrophs

129
Q

removal of electrons from a substance, usually hydrogen atoms

A

oxidation

130
Q

addition of electrons to a substance through addition of hydrogen atoms

A

reduction

131
Q

study of changes in energy that accompany events in the universe

A

thermodynamics

132
Q

applies principles of thermodynamics to the biological world

A

bioenergetics

133
Q

restricted portion of the universe that is being considered

A

system

134
Q

the rest of the universe

A

surroundings

135
Q

sealed from is environment and cannot take in nor release energy

A

closed system

136
Q

can have energy added to it or removed from it

A

open system

137
Q

each of its variable properties is held at a specified value

A

state

138
Q

the use of energy to drive a process other than heat flow

A

work

139
Q

the amount of energy required to raise one gram of water by one degree centigrade at one atmosphere of pressure

A

calorie

140
Q

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

A

first law of thermodynamics

141
Q

total energy stored within a system

A

internal energy

142
Q

heat content is exalted to E, dependent on pressure and volume

A

enthaply

143
Q

energy is released; deltaH is negative

A

exothermic

144
Q

energy is absorbed; deltaH is positive

A

endothermic

145
Q

a favorable reaction and can occur without the input of external energy

A

thermodynamically spontaneous reaction

146
Q

a measure of whether of not a reaction or process can occur

A

thermodynamic spontaneity

147
Q

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

A

second law of thermodynamics

148
Q

randomness or disorder

A

entropy

149
Q

measure of spontaneity for a system alone; readily measurable indicator of spontaneity

A

free energy

150
Q

reactions are energy-yielding and occur spontaneously

A

exergonic

151
Q

reactions are energy-requiring and do not occur spontaneously under the conditions specified

A

endergonic

152
Q

a reaction can take place, not that it will; usually an input of activation energy is required

A

spontaneous

153
Q

measure of directionality

A

equilibrium constant

154
Q

25C
1 atm
1M
pH 7

A

standard state

155
Q

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

A

standard free energy change

156
Q

concentrations of reactants and products remain relatively constant, but not at equilibrim

A

steady state

157
Q

all cellular processes or reactions are mediated by protein catalysts

A

enzyme catalysis

158
Q

the minimum amount of energy required before collisions between the reactants will give rise to products

A

activation energy

159
Q

intermediate chemical stage which has a free energy higher than that of the initial reactants

A

transition state

160
Q

molecules that are thermodynamically unstable but do not have enough energy to exceed the activation energy barrier

A

metastable state

161
Q

enhances the rate of a reaction by providing such a surface and lowering Ea

A

catalyst

162
Q

three properties of catalysts

A

increase reaction rate by lowering the Ea required
form transient, reversible complexes with substrate molecules
change the rate which equilibrium is achieved

163
Q

a characteristic cluster of amino acids

A

active site

164
Q

inorganic enzyme conjugates

A

cofactors

165
Q

organic enzyme conjugates

A

coenzymes

166
Q

ability to discriminate between very similar molecules

A

substrate specificity

167
Q

enzymes accept any of an entire group substrates sharing a common feature

A

group specificity

168
Q

enzyme holds substrate in the optimal position for reaction

A

substrate orientation

169
Q

substrate binding at the active site induces a conformational change in the shape of the enzyme

A

induced-fit model

170
Q

the study of rate of enzymatic factions under various experimental conditions

A

enzyme kinetics

171
Q

measured over a brief time during which the substrate concentration has not yet decreases enough to affect the rate of reaction

A

initial reaction rate

172
Q

rate of change in product concentration per unit time

A

initial reaction velocity

173
Q

as [S] tends toward infinity, v. approaches an upper limiting value

A

maximum velocity

174
Q

inability of increasingly higher substate concentrations to increase the faction velocity beyond a finite upper value

A

saturation

175
Q

the concentration of substrate that gives half maximum velocity

A

Km

176
Q

rate at which substrate molecules are converted to product by a single enzyme at maximum velocity

A

turnover number Kcat

177
Q

compounds that resemble real substrates or transition states closely enough to occupy the active site but not closely enough to complete the reaction

A

substrate analogs and transition state analogs

178
Q

bind the enzyme covalently and cause permanent loss of catalytic activity

A

irreversible inhibitors

179
Q

bind enzymes noncovalently and can dissociate from the enzyme

A

reversible inhibitors

180
Q

bind the active site of an enzyme and compete with substrate for the active site

A

competitive inhibitors

181
Q

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

A

noncompetitive inhibition

182
Q

depends on interactions of substrates and products with an enzyme

A

substrate-level regulation

183
Q

the single most important control mechanism whereby the rates of enzymatic reactions are adjusted to meet the cell’s needs

A

allosteric regulation

184
Q

have two conformations one in which it has affinity for the substrate and one in which it does not

A

allosteric enzymes

185
Q

makes use of this property by regulating the conformation of the enzyme

A

allosteric regulation

186
Q

regulates enzyme activity by binding and stabilizing one of the conformations

A

allosteric effector

187
Q

allosteric effector binds a site distinct from the active site

A

allosteric (or regulatory) site

188
Q

active and allosteric sites are on different subunits

A

catalytic and regulatory subunites

189
Q

conformation change increases affinity for substrate

A

positive cooperativity

190
Q

affinity for substrate is decreased

A

negative cooperativity

191
Q

final product of an enzyme pathway negatively regulates an earlier step in the pathway

A

feedback inhibition

192
Q

enzymes are subject to this

activity is regulated by addition or removal of groups, such as phosphate, methyl, acetyl groups etc.

A

covalent modification

193
Q

reversible addition of phosphate groups

A

phosphorylation

194
Q

catalyze the phosphorylation of other proteins

A

protein kinases

195
Q

removal of phosphate groups from proteins

A

dephosphorylation

196
Q

catalyze the dephosphorylation of other proteins

A

protein phosphatases

197
Q

activation of a protein by a one-timid irreversible removal of part of the polypeptide chain

A

proteolytic cleavage

198
Q

RNA molecules that have catalytic activity

A

ribozymes

Cell Molec (1 decks)

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