FINAL EXAM Flashcards

(582 cards)

1
Q
A
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2
Q

What are the properties of life?

A

1.Order
2.Regulation
3.Growth/Development
4.Metabolism
5.responsivness
6.Reproduction
7.Evolution

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3
Q

Levels of Biological Organization?

A

Molecules & Atoms
Organelle
Cell: The fundamental unit of life.
Tissue
Organs
Organ System
Organism
Population
Community
Ecosystem
Biosphere

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4
Q

Taxonomy Classifications

A

Domain, Kingdom, Phylum, Class, Order, Family, Genus, Species

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5
Q

Three Domains

A

Bacteria: Prokaryotic organisms.
Archaea: Prokaryotic organisms, often living in extreme environments.
Eukarya: Eukaryotic organisms.

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6
Q

Bacteria

A

Prokaryotic organisms.

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7
Q

Archea

A

Prokaryotic organisms, often living in extreme environments.

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8
Q

Eukarya

A

Eukaryotic organisms.

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9
Q

Prokaryotes

A

Smaller cells
less complex structure
No nucleus
always single cell
not membrane bound (true organelle)

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10
Q

Eukaryotes

A

Bigger Cells
More complex structure
nucleus
can be single or multi
have organelles

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11
Q

Evolution

A

species change over time for success

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12
Q

Natural Selection

A

Process by which evolution occurs.
-overproduction and comp
-individual variation
-unequal reproductive success

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13
Q

Scientific Method

A

Observation
Question
Hypothesis: A testable, proposed explanation.
Prediction: An “if…then” statement based on the hypothesis.
Experiment: A procedure to test the prediction.

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14
Q

Matter

A

anything that has mass and takes up space

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15
Q

Element

A

a pure substance consisting of only one type of atom

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16
Q

Compunds

A

a substance containing two or more elements in a fixed ratio

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17
Q

Atom

A

smallest, stable unit of an element

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18
Q

atomic theory

A

1.Matter is composed of atoms
2.Atoms in each element are different than those of other elements
3.Chemical compounds made of atoms in specfic ratios
4.Chemical reactions change the way atoms are combined;Atoms are unchanged

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19
Q

Proton

A

positive charge, 1 AMU, in nucleus

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20
Q

Neutron

A

no charge, 1 AMU, in necleus

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21
Q

Electron

A

negative charge, very small mass

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22
Q

Atomic number

A

upper left
=to # of protons

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23
Q

Atomic mass

A

mass - atomic #
protons+neutrons

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24
Q

Isotope

A

same elements, different mass

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25
Radioactive isotopes
unstable, nucleus decays spontaneously giving off particles and energy
26
Periodic table
periods=rows groups=columns Main group elements 1A-8A
27
Electron shells
1st. lowest energy, Max 2 electrons 2nd. Next highest, Max 8 electrons 3rd. Highest energy. Max 8
28
Valence Shell
-outermost occupied shell -if valence shell has missing electrons, more prone to form bonds/compounds
29
Covalent bond
Shared electrons
30
Double bond
sjared 4 electrons
31
Triples bond
Shared 6 electrons
32
Ionic bond
transfer of electrons
33
Hydrogen bond
between opposite poles of charged (polar) molecules (weakest bonds)
34
Electro negativity
Amount of E- attraction of atom in covalent bond
35
Non polar
Even electron sharing
36
Polar
Uneven electron sharing
37
Ion
Atom that has gained or lost 1 or more electrons
38
Anion
neg charge
39
cation
Pos charge
40
Ionic Compounds
Salts
41
Reactants
start
42
Products
end
43
Types of reactions
Precipitation acid-base neutrlazation Redox=oxidations-reduction
44
Potential
stored/postion
45
kinetic
motion
46
thermal
the kinetic energy of molecules
47
tempurature
measurment of thermal energy
48
heat
thermal energy transfer
49
Solid
def shape, def vol, organized @ molecular level, Molecules very close, little movement
50
Liquid
Def vol, no def shape, not organized, molecules are close, moderate shape
51
Gas
no def vol or shape, not organized, molecules are far apart, lots of movement
52
Vaporization
amount of heat to completely vaporize liquid after boiling
53
Heat of fusion
amount of heat to completely melt solids after melting point
54
Chemical Changes
chemical bonds are broken or formed, changes chemical makeup
55
Solution
homogenous mix tiny particles
56
solvent
substance in which something is dissolved
57
solute
thing dissolved in solvent
58
aqueous solution
a solution in which water acts as solvent
59
special properties of water
1.polar 2.cohesive 3.high surface tension 4.high heat capacity 5.high heat of vaporization 6.good solvent 7.ice floats
60
molarity=(M)
mol/L
61
Acid
Provide hydrogen ions in water. strong release ions easily, weak is opposite
62
Base
can accept hydrogen ions in water. strong holds ions tightly, weak opp
63
PH
Logarithmic measure of the concentration of hydrogen ions.
64
PH #
1-14. less than 7 is acid more than 7 is base example PH 14 has 10^-14 hydrogen ions
65
Buffer
Combo of substances that prevent/resist a drastic change in PH. Roughly equal mix of weak acid and its conjugate base
66
67
Major elements of organic molecules
C,H,O,N
68
Hydrocarbons
only C+H
69
isomer
molecules with the same molecular formulas, but different arrangements of atoms
70
Cisisomer
two X's on the same side
71
Transisomer
two X's on opposite sitdes
72
enantiomers
mirrored X's
73
Structural isomer
molecule with the same chemical formula as another molecule but a different atomic arrangement, meaning the atoms are connected in a different order
74
Hydrolysis
Breaking down a polymer w/ aid of water
75
dehydration synthesis
chemical reaction that joins two molecules together to form a larger, more complex molecule by removing a water molecule (H₂O) in the process
76
Carbohydrates
Contain C,O,H w/ multi hydroxyl groups, alot made by plants
77
Monosaaccharide
simple sugar/reducing surgar building block of carbs
78
Important Monosaccharides
Pentoses-5carbons, deoxyribose, ribose Hexoses-6 carbons, glucose, fructose, galactose
79
Glysidic bond
Joins 2 sugars
80
Disaccharide
2 monosacs, simple sugars not reducing
81
Maltose
2 glucose
82
lactose
galactose, glucose
83
sucrose
fructose and glucose
84
Starch
big molecules, made by plants, 2 molecules, 20%amylose +80%amylopectin
85
glycogen
how animals store energy for later, stored in liver&muscle, up to 1 million glucose
86
Cellulose
in the walls of plants, humans cannot digest
87
Chitin
found in incesct exoskeleton and fungal walls
88
peptidoglycan
found in bacteria cell walls
89
Fatty Acids
building blocks of lipids 12-22 carbons carboxyl groups on 1 end non polar hydrophobic uncharged
90
Saturated fatty acids
no double bonds solid @ room temp Stack easily max# of hydrogens
91
Unsaturated fatty acids
atleast 1 double bond liquid at room temp dont stack tightly fewer hydrogens
92
Triglyceride
glycerol+3 fatty acids
93
Phospholipid
only 1 glycerol 2 fatty acids organic group attached by a phosphate group charged heads
94
Sterols
have 4 ring steroid nucleus
95
steroid hormones
Estrogen, testosterone, cortisol
96
Ammino acids
Building blocks of protein Every amino acid has amino group &carboxyl group and variable side chain (r) held together by peptide bond/amide bond
97
Functions of proteins in organisms
1.enzymes 2.storage of amino acids 3.Transport of sub in cell mem 4.defense against disease 5.hormone 6.receptor 7.structure 8.motor
98
20 amino acids
Alanine Ala A Arginine Arg R Asparagine Asn N Aspartic Acid Asp D Cysteine Cys C Glutamine Gln Q Glutamic Acid Glu E Glycine Gly G Histidine His H Isoleucine Ile I Leucine Leu L Lysine Lys K Methionine Met M Phenylalanine Phe F Proline Pro P Serine Ser S Threonine Thr T Tryptophan Trp W Tyrosine Tyr Y Valine Val V
99
Primary protein structure
chain of amino acids
100
Secondary Protein Structure
local folding, alpha helix, beta pleated
101
Tertiary structure
Overll/global folding
102
Quaternary structure
only some proteins have. only when more than one poly peptide
103
Denaturation
unfolding of protein loses function
104
chaperonin
complex that helps protein fold
105
DNA to RNA to Protein
transcribed translated
106
DNA
Deoxyribonucleic acid Deoxyribose Usually double strand tymine
107
RNA
Ribonucleic acid Ribose Uracil usually single strand both have a,c,g
108
Purines
adenine, guanine
109
Pyrimidines
cytosine, thymine, uracil
110
DNA AND RNA DIFFER
the monosac U v T SS v s
111
anti parallel
DNA strands face opposite ways
112
ATP
adenosine triphosphate. favorite way for cells to transfer energy
113
Prokaryotes
Domains: Bacteria, Archaea Key Structures: Nucleoid (DNA region, no membrane) Ribosomes (protein synthesis) Cell membrane (phospholipid bilayer) Cell wall (peptidoglycan in bacteria) Surface-to-volume ratio: Higher ratio = more efficient exchange.
114
Eukaryotes
Domains: eukarya (kingdoms animalia, plantae, fungi) Main Components: Plasma Membrane: Selective barrier Cytoplasm: Cell contents outside nucleus Cytosol: Fluid part of cytoplasm Organelles: Specialized functions
115
nucleus
Nuclear envelope (double membrane seperated by 20-40nanometers) Chromatin (DNA + histone proteins) → Chromosomes Nucleolus (makes rRNA & ribosomes)
116
Ribosomes
40% protein, 60% rRNA; protein synthesis
117
Endoplasmic reticulum
Rough ER: Ribosomes attached, protein synthesis, glyco proteins, secretory proteins, membrane proteins, some phospholipids Smooth ER: Lipid synthesis, detoxification
118
Golgi Complex
Modifies, sorts, ships proteins
119
Vesicles
Transport substances
120
lysosomes
Digestive enzymes, waste breakdown
121
Vacuoles
storage (eg water in plants)
122
peroxisomes
breakdown fatty acids, detoxify
123
Mitochondria
ATP production Cristae(folds) Matrix (inner fluid) Inner/outer membranes
124
Chloroplast
photosynthesis own DNA and RIBOSOMES Thylakoids(disks) Grana (stacks) Stroma (fluid)
125
Endosymbiotic theory
Mitochondria and chloroplasts evolved from bacteria
126
Microfilaments (actin)
cell shape, movement Form 4nm rods
127
Microtubules(Tubulin)
Transport organelles around, cell division 25nm in diameter
128
Intermiediate filaments
structural support 10nm most common protein keratin
129
Centrosome organize Microtuble
made of two centrioles and always at right angle
130
Flagells
in eukaryotes whip-like,
131
cillia
short, hair-like appendages on the surface of eukaryotic cells that are crucial for both cell movement and sensing the environment.
132
cell wall
Animals cells do not have cell walls so be careful (when we mean cell membrane say it and not wall) in plants the walls are made of cellulose In fungi it can be cellulose, and or ketone, and or glycomanin Algae can have cellulose, auger, karagenin, pectinmanins, and some have some made of minerals
133
Bacteria
peptidoglycan
134
Cell membrane functions
Protect/barrier Regulate echange w/ enviroment Communication structure
135
Glycolipid
lipid w/ carbs attached
136
Glycoprotein
Protein with carbs attached
137
Integral protein
embedded in phospholipid bilayer
138
peripheral
not embedded
139
Fluid mosaic model
not uniform
140
uniport
lets one thing through along concentration gradient
141
symport
lets 2 things going in the same direction. one with and one against concentration gradiaent
142
antiport
1 going in, 1 going out, one with and one against concentration gradient
143
Lipid bilayer
hydrophobic tails, hyrdrophillic heads
144
Transmembrane
span entire membrane
145
Protein functions
transport Receptors (signal detection) Enzymes (catalysis) Linkers (attachment) Cell identity markers (recognition)
146
Glycocalyx
Glycoproteins + glycolipids → cell recognition & adhesion a thin, carbohydrate-rich layer that covers the surface of all cells in the body
147
osmosis
diffusion of water
148
tonicity
Isotonic: No net water movement Hypotonic: Water enters cell (lysis in animals, turgid in plants) Hypertonic: Water leaves cell (crenation in animals, plasmolysis in plants)
149
Passive transport
Diffusion, Facilitated diffusion(channels, carriers), no energy req
150
Active transport
Requires ATP Electrochemical gradients Against gradient
151
Contransport
symport and antiport
152
exocytosis
materials exit cell
153
endocytosis
materials enter cell
154
phagocytosis
process in which cells engulf and destroy foreign particles, such as bacteria, dead cells, and debris
155
pinocytosis
the uptake of extracellular fluids and dissolved solutes, such as fat droplets, vitamins, and antigens.
156
receptor mediated
specific molecules (ligands) bind to cell surface receptors, triggering their uptake into the cell.
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158
What are cell junctions?
Contact points between different cells in a multicellular organism (tissues)
159
What are plasmodesmata and where are they found?
Found only in plants, plasmodesmata are channels between adjacent cells allowing faster communication
160
What proteins make up tight junctions?
Occludins and claudins
161
Function of tight junctions?
Prevent separation under stress and prevent leakage between cells
162
What proteins form adherens junctions?
Cadherins (attached to microfilaments inside the cell)
163
Function of adherens junctions?
Form a belt of attachment and prevent separation under stress
164
What proteins form desmosomes?
Cadherins attached to intermediate filaments
165
Function of desmosomes?
Prevent separation, act like “buttons” attaching cells in certain spots
166
What proteins form hemidesmosomes?
Integrins attaching to extracellular matrix and intermediate filaments
167
Function of hemidesmosomes?
Anchor cells to extracellular material, like “half desmosomes”
168
What proteins form gap junctions?
Connexins
169
Function of gap junctions?
Form channels for communication between cells, animal equivalent of plasmodesmata
170
What does the 1st law of thermodynamics state?
Energy can be transferred and transformed, but cannot be created or destroyed (law of conservation of energy)
171
What does the 2nd law of thermodynamics state?
Every energy transfer increases entropy (S), the measure of randomness/disorder
172
What is entropy (S)?
Measure of disorder; higher in gases, lower in solids
173
What is enthalpy (H)?
Measure of energy associated with substances in a reaction (heat of reaction)
174
Exothermic vs. Endothermic reaction?
Exothermic = negative ΔH (heat released). Endothermic = positive ΔH (heat absorbed)
175
What makes a reaction spontaneous?
Negative ΔH (heat released) and positive ΔS (entropy increases)
176
What is activation energy?
Energy barrier needed to start a reaction
177
What factors affect reaction rate?
Temperature, concentration of reactants/products, catalysts
178
What is a catalyst?
Substance that accelerates a reaction without being used up (enzymes in biology)
179
What is chemical equilibrium?
State where concentrations of reactants and products remain constant
180
What is Le Châtelier’s principle?
When stress is applied to equilibrium, the system shifts to counteract stress
181
Define catabolism.
Breaking down molecules (e.g., proteins → amino acids)
182
Define anabolism.
Building molecules (e.g., amino acids → protein)
183
How much energy does hydrolysis of ATP release?
7.3 kcal/mol
184
What are enzymes?
Biological catalysts that lower activation energy, increase reaction rate, are specific, regulated, efficient, and made of proteins
185
What is an active site?
Region where substrate binds; enzyme may change shape slightly (induced fit)
186
What are cofactors and coenzymes?
Cofactors = non-protein helpers (inorganic ions). Coenzymes = organic molecules (often vitamins)
187
Apoenzyme vs. Holoenzyme?
Apoenzyme = inactive enzyme without cofactor. Holoenzyme = active enzyme with cofactor
188
Factors affecting enzyme activity?
Concentration, temperature (denaturation risk), pH (optimal range), inhibitors
189
What is a competitive inhibitor?
Binds in active site but not a substrate, blocking substrate
190
What is a noncompetitive inhibitor?
Binds elsewhere on proteins, changing enzyme shape
191
What sets the overall rate of a metabolic pathway?
The slowest step (rate-limiting step)
192
What is the overall chemical reaction for photosynthesis?
6 CO2 + 6 H2O + light energy → C6H12O6 + 6 O2. Carbon dioxide and water combine using light energy to produce glucose and oxygen.
193
Define autotroph.
An **autotroph** is an organism that makes its own food from inorganic sources, such as CO2 and water, using light or chemical energy.
194
Define heterotroph.
A **heterotroph** is an organism that must obtain energy by consuming other organisms or organic molecules.
195
Define producer and consumer.
A **producer** (autotroph) creates its own food using sunlight or chemicals, while a **consumer** (heterotroph) must eat producers or other consumers for energy.
196
What is the function of stomata?
**Stomata** are pores on the underside of leaves that allow for **gas exchange**—CO2 enters, and O2 and water vapor exit.
197
Where does photosynthesis take place in the cell?
Photosynthesis occurs in the **chloroplasts** of plant cells, mainly within the **mesophyll** tissue of leaves.
198
What are the two stages of photosynthesis and where do they occur?
1) **Light-dependent reactions** – occur in the **thylakoid membranes**; convert light energy to ATP and NADPH. 2) **Calvin cycle (light-independent reactions)** – occurs in the **stroma**; uses ATP and NADPH to fix CO2 into sugar.
199
What colors of light are most effective for photosynthesis?
**Red and blue light** are most effective for photosynthesis because they are absorbed by chlorophyll pigments, while **green light** is least effective because it is reflected.
200
What is the wavelength range of visible light?
Visible light ranges from about **380 to 750 nanometers (nm)**.
201
What are the main photosynthetic pigments in plants?
The main pigments are **chlorophyll a**, **chlorophyll b**, and **carotenoids**. Chlorophyll a is the primary pigment; chlorophyll b and carotenoids are accessory pigments.
202
What is the structural difference between chlorophyll a and chlorophyll b?
**Chlorophyll a** has a **CH3 group**, while **chlorophyll b** has a **CHO group** on its porphyrin ring.
203
What role do carotenoids play in photosynthesis?
**Carotenoids** absorb wavelengths not absorbed by chlorophyll and protect the plant from excess light by acting as **photoprotective pigments**.
204
What happens when a photon hits a pigment molecule?
The photon excites an electron to a **higher energy level**; this energy is transferred through pigment molecules until it reaches the **reaction center**.
205
What is a photosystem?
A **photosystem** is a complex of pigments and proteins that captures light energy. It contains a **reaction center** with a special pair of chlorophyll molecules and a **primary electron acceptor**.
206
What are the two types of photosystems in photosynthesis?
**Photosystem II (PSII)** with a reaction center called **P680**, and **Photosystem I (PSI)** with a reaction center called **P700**.
207
What is the function of Photosystem II?
**PSII** captures light energy to **split water molecules (photolysis)**, releasing **O2**, **protons (H⁺)**, and **electrons** that enter the electron transport chain.
208
How many photons are required to split two water molecules?
It takes **four photons** to split **two H2O molecules** into O2, 4 H⁺, and 4 e⁻.
209
What is the electron transport chain in photosynthesis?
A series of carriers including **plastoquinone (Pq)**, **cytochrome complex**, and **plastocyanin (Pc)** that move electrons from PSII to PSI, creating a **proton gradient** used for ATP synthesis.
210
What is the function of Photosystem I?
**PSI** receives electrons from the ETC and re-energizes them with light energy to reduce **NADP⁺ to NADPH**.
211
What are the two main energy products of the light reactions?
**ATP** and **NADPH**, which are used in the **Calvin cycle** to power carbon fixation.
212
How is ATP produced during the light reactions?
ATP is produced by **chemiosmosis** when **ATP synthase** uses the **proton gradient** created across the thylakoid membrane to phosphorylate ADP.
213
Where are the light reactions located?
In the **thylakoid membranes** of the chloroplast.
214
What is the role of NADPH in photosynthesis?
**NADPH** provides high-energy electrons and reducing power for the **Calvin cycle** to synthesize carbohydrates.
215
What is the Calvin cycle?
The **Calvin cycle** (light-independent reactions) uses **CO2**, **ATP**, and **NADPH** to produce **G3P (glyceraldehyde-3-phosphate)**, a precursor to glucose.
216
What are the three main phases of the Calvin cycle?
1) **Carbon fixation** by **RuBisCO** enzyme attaching CO2 to RuBP. 2) **Reduction** phase using ATP and NADPH to form G3P. 3) **Regeneration** of RuBP from G3P using ATP.
217
What enzyme catalyzes carbon fixation in the Calvin cycle?
**RuBisCO** (ribulose bisphosphate carboxylase/oxygenase) catalyzes the reaction of CO2 with **RuBP**.
218
How many CO2 molecules are needed to produce one G3P?
It takes **3 CO2 molecules** to produce **one G3P** (three turns of the Calvin cycle).
219
How many CO2 molecules are needed to produce one glucose molecule?
It takes **6 CO2 molecules** (six turns of the Calvin cycle) to produce one molecule of glucose.
220
What are the inputs and outputs of the Calvin cycle?
**Inputs:** CO2, ATP, NADPH. **Outputs:** G3P (sugar), ADP, NADP⁺, and inorganic phosphate (Pi).
221
What is the relationship between the light reactions and the Calvin cycle?
The **light reactions** provide **ATP and NADPH** to power the **Calvin cycle**, which returns **ADP, Pi, and NADP⁺** back to the light reactions.
222
What is C3 photosynthesis?
**C3 photosynthesis** is the normal Calvin cycle pathway where CO2 is fixed directly by RuBisCO to form a 3-carbon compound (3-phosphoglycerate).
223
What problem can occur in C3 plants?
In hot, dry conditions, **photorespiration** occurs when RuBisCO binds O2 instead of CO2, wasting energy and reducing photosynthetic efficiency.
224
What is C4 photosynthesis?
**C4 plants** (e.g., corn, sugarcane) fix CO2 into a 4-carbon compound using **PEP carboxylase** in mesophyll cells, then transport CO2 to bundle-sheath cells for the Calvin cycle.
225
Why is C4 photosynthesis advantageous?
It **minimizes photorespiration** and increases CO2 concentration for RuBisCO, improving efficiency in **hot, sunny climates**.
226
What is CAM photosynthesis?
**CAM (Crassulacean Acid Metabolism)** plants (e.g., cacti, pineapple) open **stomata at night** to fix CO2 into organic acids, then close stomata during the day to conserve water.
227
Why is CAM photosynthesis advantageous?
It conserves water in **arid environments** by separating CO2 uptake (night) and Calvin cycle (day) by time.
228
What is the relationship between photosynthesis and cellular respiration?
Photosynthesis **stores energy** in glucose molecules by using CO2 and H2O, while cellular respiration **releases energy** by breaking down glucose into CO2 and H2O. They are **complementary processes** in the carbon and energy cycles.
229
What is the structure of DNA?
Double helix composed of two antiparallel strands of nucleotides.
230
What are the two classes of nitrogenous bases?
Purines (adenine, guanine) and pyrimidines (cytosine, thymine).
231
Which bases pair together in DNA?
Adenine pairs with thymine (A--T); guanine pairs with cytosine (G---C).
232
What type of bonds hold base pairs together?
Hydrogen bonds.
233
What does semiconservative replication mean?
Each new DNA molecule has one old strand and one newly synthesized strand.
234
Where does DNA replication begin?
At the origin of replication.
235
What enzyme unwinds the DNA helix?
Helicase.
236
What enzyme relieves strain ahead of the replication fork?
Topoisomerase.
237
What are single-strand binding proteins (SSBPs)?
Proteins that stabilize unwound DNA strands and prevent reannealing. Keep Fork Open
238
What is the replication fork?
Y-shaped region where DNA is unwound and new strands are synthesized.
239
What enzyme synthesizes the RNA primer?
Primase.
240
What is the function of an RNA primer?
Provides a short RNA segment with a free 3′-OH group for DNA polymerase to extend.
241
Which enzyme adds new nucleotides during replication?
DNA polymerase III.
242
In what direction does DNA replication occur?
Always in the 5′ to 3′ direction.
243
What is the leading strand?
The DNA strand synthesized continuously toward the replication fork.
244
What is the lagging strand?
The strand synthesized discontinuously away from the fork in short Okazaki fragments.
245
What are Okazaki fragments?
Short segments of DNA formed on the lagging strand.
246
Which enzyme removes RNA primers and replaces them with DNA?
DNA polymerase I.
247
What enzyme seals gaps between fragments?
DNA ligase.
248
DNA Ligase
Connects Sugar Phosphate Backbone
249
What is the rate of DNA replication?
≈500 bp/sec in bacteria; ≈50 bp/sec in eukaryotes.
250
How many origins of replication are found in prokaryotes and eukaryotes?
Prokaryotes: one origin per chromosome; eukaryotes: multiple origins per chromosome.
251
What enzymes proofread DNA for errors?
DNA polymerases.
252
What enzyme removes damaged sections during DNA repair?
Nuclease.
253
Which enzymes fill in the gap after nuclease excision?
DNA polymerase and DNA ligase.
254
What are mutations?
Permanent changes in the DNA sequence.
255
What are telomeres?
Protein bind single standed section protects genes near end of chromosome(human repeat = TTAGGG).
256
What is the function of telomerase?
Extends telomeres to compensate for shortening during replication.
257
Which cells have active telomerase?
Germ cells, stem cells, and some cancer cells.
258
Define nucleosome.
DNA wrapped around histone protein cores.
259
What is chromatin?
Complex of DNA and proteins forming chromosomes.
260
What is heterochromatin?
Tightly packed, transcriptionally inactive chromatin.
261
What is euchromatin?
Loosely packed, transcriptionally active chromatin.
262
What is the purpose of cell division?
Cell replacement, tissue renewal, growth, development, and asexual reproduction.
263
Give three examples of asexual reproduction.
Amoeba reproduction, regeneration of a sea star, growth from a plant clipping.
264
Define genome.
All the genetic material in a cell.
265
Define chromosome.
A single DNA molecule associated with proteins that contains genetic information.
266
Define chromatin.
The complex of DNA and proteins that makes up chromosomes.
267
What are somatic cells?
Body cells that are diploid (2n) normal cell
268
Define sister chromatids.
Identical copies of a chromosome joined at a centromere.
269
Define centromere.
The region where sister chromatids are attached.
270
List the main stages of the cell cycle.
Interphase (G1, S, G2) and Mitotic phase (Mitosis and Cytokinesis).
271
What happens during G1 phase?
Duplicating organelles. 8-10hr
272
What happens during S phase?
DNA replication occurs. 8 hourd
273
What happens during G2 phase?
Cell prepares for division
274
What occurs during the Mitotic phase?
Cell division
275
List the stages of mitosis.
Prophase, Metaphase, Anaphase, Telophase.
276
What happens during prophase?
Chromosome condenses and the mitotic spindle begins to form and nuclear envelope breaks down
277
What happens during late prophase?
Nuclear envelope breaks down and spindle fibers attach to kinetochores.
278
What happens during metaphase?
Chromosomes align at the metaphase plate.
279
What occurs during anaphase?
Sister chromatids separate and move toward opposite poles.
280
What occurs during telophase?
Nuclear membranes reform and chromosomes begin to decondense.
281
Define mitotic spindle.
A structure made of microtubules that separates chromosomes during mitosis.
282
Define kinetochore.
A protein structure on chromatids where spindle fibers attach.
283
What is cytokinesis?
Division of the cytoplasm to form two daughter cells.
284
How does cytokinesis differ between animal and plant cells?
Animal cells form a cleavage furrow; plant cells form a cell plate.
285
What is binary fission?
A type of asexual reproduction used by bacteria to divide.
286
What molecules control the cell cycle?
Cyclins and cyclin-dependent kinases (Cdks) which form MPF (maturation/mitosis promoting factor).
287
Name the three major checkpoints in the cell cycle.
G1 checkpoint, G2 checkpoint, and M (Anaphase) checkpoint.
288
What happens at the G1 checkpoint?
Determines whether the cell will divide or enter G0 phase.
289
What happens at the G2 checkpoint?
Checks for DNA damage and proper replication before mitosis.
290
What happens at the M checkpoint?
Ensures all chromosomes are properly attached to spindle fibers before separation.
291
What is PDGF?
Platelet-derived growth factor that stimulates cell division.
292
Define density-dependent inhibition.
Cells stop dividing when they become crowded.
293
Define anchorage dependence.
Cells must be attached to a surface to divide.
294
What are somatic cells?
Body cells that are diploid (2n).
295
What are gametes?
Sex cells (sperm and egg) that are haploid (1n).
296
Define diploid.
Cells with two sets of chromosomes (2n).
297
Define haploid.
Cells with one set of chromosomes (1n).
298
What is a zygote?
The fertilized egg formed by the fusion of gametes.
299
Define karyotype.
micrograph of metaphase, chromosomes arrangeed in homologous pairs
300
What determines biological sex in mammals?
XX = female, XY = male.
301
What are autosomes?
Non-sex chromosomes (chromosomes 1–22 in humans).
302
What are the three types of sexual life cycles?
Animal, only haploid cells are gametes, alternation of generations, and diploid only occurs in the zygote.
303
What happens in Meiosis I?
Homologous chromosomes separate.
304
What happens in Meiosis II?
Sister chromatids separate.
305
Describe Prophase I.
Homologous chromosomes pair up (synapsis) and crossing over occurs.
306
Describe Metaphase I.
Homologous pairs align at the metaphase plate.
307
Describe Anaphase I.
Homologous chromosomes move to opposite poles.
308
Describe Telophase I.
Two haploid cells form; chromosomes are still double.
309
What happens in Anaphase II?
Sister chromatids finally separate.
310
Define crossing over.
Exchange of genetic material between homologous chromosomes.
311
List three sources of genetic variation.
Independent assortment, random fertilization, and crossing over.
312
Define heredity.
The transmission of traits from parents to offspring.
313
Define genetics.
The study of heredity and variation.
314
Define character.
A heritable feature that varies among individuals.
315
Define trait.
A variant of a character.
316
Who is Gregor Mendel?
A monk who discovered the basic principles of heredity using pea plants.
317
Define true-breeding.
Plants that produce offspring identical to themselves.
318
Define hybrid.
Offspring of crosses between parents with different traits.
319
Define genetic cross.
Mating of two organisms to study inheritance.
320
Define parental generation.
The P (or F0) generation in a genetic cross.
321
Define F1 generation.
The hybrid offspring of the parental generation.
322
Define F2 generation.
The offspring of F1 individuals.
323
What is a monohybrid cross?
A cross that studies inheritance of one trait.
324
Define allele.
Alternative versions of a gene that account for variations in inherited characters.
325
State Mendel’s Law of Segregation.
1. Alternative versions of genes account for variations in inherited character we call these alleles 2. For each inherited character, an organism inherits two alleles, one from each parent 3. if the two alleles differ, one determines the trait, called the dominant allele. other is not detectable, called recessive allele. 4. Sperm and egg carries only one allele for each character. the twi alleles seperate during gamete production
326
Define homozygous.
Having two identical alleles for a gene.
327
Define heterozygous.
Having two different alleles for a gene.
328
Gene
Segment of DNA that codes for a trait, RNA
329
Phenotypic ratio
The ratio of visible traits that appear in offspring after a genetic cross (e.g., 3:1 in a monohybrid cross)
330
Genotypic ratio
The ratio of genetic combinations of alleles among offspring (e.g., 1 AA : 2 Aa : 1 aa)
331
Purpose of a testcross
To determine the genotype of an organism expressing a dominant trait by crossing it with a homozygous recessive individual
332
Dihybrid cross definition +
A cross between parents differing in two traits, tracking inheritance of two genes simultaneously
333
Law of independent assortment +
Genes for different traits separate independently during gamete formation if they are on different chromosomes
334
Does dominant mean most common
No, dominant alleles can be rare in a population
335
Complete dominance
One allele completely masks the effect of another in heterozygotes
336
Incomplete dominance
The heterozygote shows a blended intermediate phenotype between the two homozygous forms
337
Codominance
Both alleles in a heterozygote are fully expressed without blending (e.g., AB blood type)
338
Why some genes have more than two alleles
Many genes have multiple possible variants in a population, such as the ABO blood group system
339
ABO blood type alleles
IA, IB, and i — IA and IB are codominant, i is recessive
340
Pleiotropy
A single gene influences multiple phenotypic traits
341
Epistasis
Interaction where one gene affects or masks the expression of another gene
342
Example of epistasis in Labradors
B/b determines pigment color, E/e controls pigment deposition — ee prevents pigment causing yellow coat
343
Polygenic inheritance
A trait controlled by two or more genes with additive effects (e.g., skin color, height)
344
Quantitative character +
A trait that varies along a continuum due to polygenic inheritance
345
Environmental effect on phenotype
Environmental conditions can influence gene expression (e.g., nutrition, temperature)
346
Family pedigree
A diagram showing inheritance of a trait through generations using standardized symbols
347
How affected individuals are shown on pedigree
Their symbol is filled in or shaded
348
Carrier definition
An individual heterozygous for a recessive disorder allele but phenotypically normal
349
Inbreeding definition
Mating between close relatives, increasing homozygosity for harmful recessive alleles
350
Example of dominant genetic disease
Achondroplasia or Huntington’s disease
351
Genetic screening methods
Prenatal testing such as amniocentesis or chorionic villus sampling, or postnatal testing
352
Chromosomal theory of inheritance
Genes are located on chromosomes + Movement of chromosomes during meiosis + fertilization accounts for inheritance patterns
353
Scientist who proved chromosomal inheritance
Thomas Hunt Morgan using fruit flies (Drosophila melanogaster)
354
Wild-type phenotype
The normal, most common form found in natural populations (denoted w⁺)
355
Mutant phenotype
A variant due to mutation that differs from the wild type
356
Sex chromosomes in mammals
XX = female, XY = male
357
X-0 sex determination system
Used by some insects (e.g., grasshoppers) XX = F X = M
358
ZW sex determination system
Used by birds and some fish ZW = F ZZ = M
359
Haplodiploid system
Found in bees and ants Females diploid Males haploid
360
Sex-linked genes
Genes located on a sex chromosome (X or Y)
361
Why X-linked disorders more common in males
Males have only one X chromosome so a single recessive allele causes the disorder
362
Examples of X-linked disorders
Red-green color blindness, Hemophilia, Duchenne muscular dystrophy
363
3 things that contribute to X-inactivation
XIST, Methylation, and barr body
364
XIST
RNA wraps around Chromosome
365
Methylation
Methylation of DNA - methyl group added to DNA molecule- CH3 Prevents Transcription
366
Barr Body
an inactivated, COndensed X chromosomes found in the somatic cells of female mammals
367
Linked genes
Genes located close together on the same chromosome; inherited together; do NOT assort independently.
368
Unlinked genes
Genes on different chromosomes OR far apart on the same chromosome; assort independently.
369
Map unit (centimorgan) linkage map
1% recombination frequency = 1 map unit (1% chance of crossing over between genes).
370
Nondisjunction
Failure of homologous chromosomes (meiosis I) or sister chromatids (meiosis II) to separate.
371
Aneuploidy
Abnormal number of chromosomes resulting from nondisjunction.
372
Monosomy
Individual has only 1 copy of a chromosome (2n − 1).
373
Trisomy
Individual has 3 copies of a chromosome (2n + 1).
374
Polyploidy
Having more than two full sets of chromosomes (3n, 4n). Common in plants.
375
Down syndrome
Trisomy 21 2 copies of ever chromosome except 21
376
Klinefelter syndrome
XXY male; sterile, may develop breast tissue.
377
XYY
Extra Y chromosome; male; usually taller; no defined syndrome.
378
XXX
XXX female; normal phenotype; sometimes taller.
379
Turner syndrome
XO female; short, sterile, poor breast development.
380
Extrachromosomal inheritance
Inheritance of genes inherited outside of norm 46 chromosomes
381
Codon
3 units that code for amino acids, 5’-3’
382
Template strand of DNA
The DNA strand used by RNA polymerase to build RNA (complementary to RNA).
383
Coding strand of DNA
Matches RNA sequence except RNA has U instead of T.
384
Why the genetic code is redundant
More than one codon can code for the same amino acid.
385
Transcription
The process of making RNA from a DNA template.
386
RNA polymerase
Enzyme that synthesizes RNA. Opens DNA, and binds to promoter
387
Promoter
DNA sequence where RNA polymerase binds to begin transcription.
388
Transcription factors
Proteins that help RNA polymerase bind to the promoter.
389
Transcription initiation complex
RNA Polymerase, 1 or more transcription factors, binds at promoter w/ tata box
390
Transcription—elongation
RNA polymerase moves 5’→3’ building RNA.
391
Transcription—termination (eukaryotes)
Polyadenylation signal causes RNA transcript to detach. Signals to add adenine at the end, 50-250, comes after stop codon
392
Rate of transcription in eukaryotes
~40 nucleotides per second.
393
RNA processing
Modifications to pre-mRNA before leaving nucleus (cap, poly-A tail, splicing).
394
Poly-A tail function and 5' cap function- modified guanine
Protects mRNA from degradation helps export from nucleus. Help ribosomes attach to 5’
395
Introns
Non-coding regions of RNA removed during RNA splicing.
396
Exons
Coding regions kept in final mRNA.
397
Spliceosome
Complex that removes introns and joins exons.
398
Ribozyme
RNA molecule that acts as an enzyme (ex: helps splice RNA).
399
Function of introns: alternative splicing
Part of intron used as exon
400
Function of introns: exon shuffling
Increases genetic variation in cross over.
401
Types of RNA: mRNA
Carries instructions Copy or a gene Uracil not thymine
402
Types of RNA: tRNA
Carries and amino acid. Hairpin loop
403
Types of RNA: rRNA
Part of ribosome, helps translation
404
Amino acid attachment site (tRNA)
Where amino acid binds to tRNA (3' end).
405
Anticodon
Complementary to the codon
406
Aminoacyl-tRNA synthetase
Enzyme that attaches the correct amino acid to tRNA (uses ATP).
407
Ribosome composition
rRNA + protein; 70S(50,30) in prokaryotes, 80S(60,40) in eukaryotes.
408
A site (ribosome)
Aminoacyl-tRNA binding site.
409
P site (ribosome)
Holds tRNA carrying the growing polypeptide chain.
410
E site (ribosome)
Exit site where uncharged tRNA leaves ribosome.
411
Start codon
AUG (codes for methionine).
412
Translation—initiation
mRNA, initiator tRNA (Met=AUG), TRANSLATION INITIATION COMPLEX.
413
Translation—elongation
Ribosome moves 5’→3’; peptide bond forms; requires 2 GTP.
414
Translation—termination
Stop codon enters A site; chain release begins.
415
Release factor
adds water to free the completed polypeptide.
416
Function of intron: regulate gene expression
Play a role in triggering a gene to/not to be transcribe
417
Functions of introns: protection
Protect from mutations and other damage to dna
418
Chaperonins
Protein complexes that assist with proper protein folding.
419
Post-translational modification
Changes to a protein after translation (cutting, adding groups, etc.).
420
Protein modification: cleavage
Part of the protein is cut off to activate it and make it functional.
421
Protein modification: adding groups
Carbohydrate, lipid, phosphate, or other chemical groups may be added to proteins.
422
Free ribosomes
Make proteins that stay and function in the cytosol.
423
Bound ribosomes (RER)
Make proteins destined for secretion, plasma membrane, or organelles (ex: lysosome).
424
Signal peptide
Short sequence on a growing polypeptide that directs ribosome to the ER.
425
SRP (signal recognition particle)
Binds to signal peptide and escorts ribosome to the ER.
426
Polyribosome (polysome)
Multiple ribosomes translating the same mRNA at once, increasing protein production.
427
Prokaryotic transcription & translation
Occur simultaneously; one mRNA may code for multiple proteins.
428
Eukaryotic transcription & translation
Not simultaneous; transcription in nucleus, translation in cytosol; mRNA codes for one protein.
429
Mutation
Permanent change in DNA sequence.
430
Point mutation
Change in one nucleotide/base.
431
Silent mutation
Change of nt, but same amino acid
432
Missense mutation
Changes in amino acid-protein change
433
Nonsense mutation
Changes amino acid to a stop codon; protein change, effect varies depending on location.(usually harmful).
434
Frameshift mutation
changes all amino acids after the mutation (usually very harmful).
435
Spontaneous mutation
Caused by DNA replication error.
436
Induced mutation
Caused by external factors (mutagens like chemicals or radiation).
437
Effects of mutations—positive
Can allow cells to adapt or gain a beneficial trait.
438
Effects of mutations—negative
Can cause loss of function; cells may not survive.
439
Gene regulation
Gene regulation is the process of turning genes on or off; controls when and how much RNA/protein is made.
440
Epigenetics
Heritable changes in gene expression that do not change the DNA sequence (e.g., chromatin modification).
441
Gene silencing
Processes that repress transcription
442
Coordinate control
When multiple genes are regulated together by the same control elements.
443
RNA interference (RNAi)
Small RNAs (miRNA, siRNA) that block translation or trigger mRNA degradation.
444
Metabolic control
Regulation of enzyme activity or regulation of transcription/translation to control metabolism.
445
Regulation of enzyme activity
Fast response: activates or inactivates enzymes already made.
446
Regulation of transcription & translation
Slower response: controls how much enzyme is produced.
447
Transcription unit (prokaryotes)
Everything that is transcribed from one promoter.
448
Operon
A cluster of genes regulated together (promoter + operator + genes).
449
Operator
DNA sequence acting as an on/off switch to signal when transcription unit is needed, In promoter region
450
Inducer
Molecule that turns on a gene that is usually OFF (common in catabolism).
451
Repressor
Protein that binds operator to turn gene expression OFF.
452
Corepressor
Molecule that activates a repressor so it can shut off the operon.
453
Repressible operon
Normally ON; turned OFF when a corepressor activates repressor (ex: trp). Binds to repressor
454
Inducible operon
Normally OFF; turned ON when inducer inactivates repressor (ex: lac).
455
Differential gene expression
Different cell types express different genes appropriate to their function
456
Chromatin modification
Chemical modifications to histones or DNA that affect transcription.
457
Histone acetylation
Adds acetyl groups (COCH3) to N-terminus; promotes transcription; Euchromatin
458
Histone methylation
Adds methyl groups (CH3); usually condenses chromatin; inhibits transcription.
459
Histone phosphorylation
Adds phosphate groups (PO4); loosens chromatin; increases transcription; euchromatin.
460
DNA methylation
Adds methyl groups to cytosine; reduces transcription; can silence genes, Can be passed to offspring
461
Epigenetic inheritance
Modifications can be inherited
462
General transcription factors
Involved in reducing transcription of genes usually active
463
Specific transcription factors
involved in increasing transcription of genes usually inactive
464
Enhancers
DNA Sequences that regulate transcription, can repress or activate.
465
Activator proteins
Bind enhancers; increase transcription of specific genes. Have DNA binding region, activation region.
466
Gene silencing (review)
Mechanisms that reduce or block transcription.
467
Alternative RNA splicing
Post-transcriptional control: different mRNAs from same gene.
468
Blocking translation
Post-transcriptional control: Regulatory proteins bind mRNA to stop ribosome binding.
469
mRNA degradation signals
Post-transcriptional control: Sequences (often 3' UTR) that control how long mRNA lasts. Pro: minutes Euk: hours to weeks
470
Phosphorylation
Adding phosphate to proteins to activate or deactivate them.
471
miRNA
Small RNA that binds mRNA to block translation or cause degradation. 22nt ss
472
siRNA
Small interfering RNA; binds to DNA triggers RNA interference and gene silencing. ds
473
Glycosylation
biological process where carbohydrate molecules (sugars or glycans) are covalently attached to proteins or lipids
474
Explain local vs long-distance cell signaling
Local: Used between adjacent or nearby cells (Paracrine, Synaptic, Cell junction). Long-distance/endocrine signaling: Hormones travel long distances in the bloodstream
475
Paracrine Signaling
Uses hormones between adjacent cells.
476
Synaptic Signaling
Used in the nervous system to send a signal from one neuron to the next.
477
Cell Junctions (Gap Junctions/Plasmodesmata)
Allow communication between adjacent cells. provides faster communication because the signal can diffuse through the gaps without having to cross two cell membranes.
478
Explain the three stages of cell signaling
-Reception: **The arrival of the signal (ligand, chemical) at the target cell** -Transduction:** The signal propagation (relay) inside the cell** -Response:**How the cell reacts to the signal.**
479
What is a Target Cell?
any cell that has a receptor for that specific signal.
480
What determines receptor location and what is the receptor structure?
Receptors are made of proteins. Cell Membrane Receptors: Located in the cell membrane. Used if the ligand is water soluble (cannot cross the membrane). Intracellular Receptors: Located in the cytoplasm or nucleus. Used if the ligand is lipid soluble (can cross the cell membrane
481
Three Major Plasma membrane receptors
GPCRs, RTKs, ligand-gated ion channels.
482
GPCR function
Occurs in cell membrane. 1.)G protein hangs out near GPCR and works with it 2.) Ligand binds to GPCR 3.) receptor changes shape 4.)activates G protein releasing GDP, Binds to GTP 5.)active G protein travels and interacts with enzyme (often adenylyl cyclase) 6.)Activated adenylyl cyclase converts ATP to cAMP and 2 phosphates 7.)signal is terminated when the G protein hydrolyzes GTP→GDP and is reset.
483
Role of adenylyl cyclase
Converts ATP to cAMP.
484
RTK function (Receptor Tyrosine Kinases)
Occurs in Cell membrane 1.) Two ligands must bind to two nearby RTKs. 2.) The two RTKs come together, forming a dimer. 3.) Once dimerized, the receptor uses 6 ATPs to phosphorylate itself (adds a phosphate to each of the six tyrosine amino acids on the inside). 4.) The fully activated RTK can then activate other proteins (relay proteins) to trigger a cellular response.
485
Role of kinases
An enzyme that add phosphates (phosphorylation).
486
Role of phosphatases
Enzyme that remove phosphates (deactivation).
487
Phosphorylation cascade
Sequential activation of kinases → leads to the amplification of the signal because one kinase can activate multiple other kinases, and so on, resulting in the binding of a single ligand activating multiple final molecules.
488
First vs second messenger and why they're important
-First = Original ligand outside cell -second = internal molecules that work inside the cell and can diffuse around like cAMP, Ca²⁺. Allow the signal to be relayed inside the cell.
489
Two second messengers
cAMP; IP3; DAG; Ca²⁺.
490
Function of Transcription factor
Turn genes on/off for final response (how the cell reacts to the signal)
491
Why same signal causes different effects
Different cells have different receptors & relay proteins that react differently to the same signal.
492
Two cytoplasmic responses
Enzyme activation; ion channel regulation.
493
Scaffolding proteins
Organize kinases to increase speed & accuracy.
494
Define apoptosis
Programmed cell death.
495
How a signal is terminated
1.)Ligand detaches; GTP→GDP 2.)phosphatases deactivate kinases 3.)cAMP degraded.
496
Genetic engineering
manipulation of genetic material (DNA) for a particular purpose.
497
Older Genetic Engineering
Older Genetic Engineering was selective breeding (selecting for certain characteristics in crops), which has been done since humans started growing crops.
498
DNA Technology
(Modern Biotech) involves more direct DNA manipulation for a particular purpose. allows us to go in, cut up DNA, put it back together, and change an organism's genetics, which is an ability we have had for only 40-50 years.
499
Origin/function of restriction enzymes
Origin/Why: naturally made by bacteria (e.g., EcoRI from E. coli, Hae3). Their original biological purpose is to fight viruses (in the bacteria they come from) by cutting the viral DNA. Function: To cut DNA in the middle ("endo-nuclease") at a specific 4-10 base pair sequence. They cut the sugar phosphate bond (the backbone).
500
Sticky vs blunt ends
Sticky = Ex. EcoRI, overhangs (DNA doesn't like to be single-stranded, so these ends are "looking for something to base pair and stick to.") blunt = Ex. Hae3, straight cuts.
501
Ligase function
Permanently connect two pieces of DNA by Sealing sugar-phosphate bonds. Why: When sticky ends form hydrogen bonds, the connection is not permanent, so ligase is needed to permanently connect the backbones.
502
Reverse transcriptase use
Makes cDNA from RNA template; no introns. **Why/origin: comes from viruses (e.g., HIV). Its use is valuable in biotech because when cDNA is made from eukaryotic mRNA, the introns have been removed. This allows the intron-free eukaryotic gene to be spliced onto a plasmid and put into bacteria (which don't have introns) to be used as a factory to make the protein.**
503
Define cDNA
Intron-free copy or complimentary DNA
504
PCR description
Amplifies a specific DNA sequence that we are interested in. via denaturation, annealing, extension.
505
PCR key enzyme & why
Taq DNA polymerase; it is thermostable and can withstand the very high temperatures required for the reaction without denaturing.
506
Primer purpose
To allow the short DNA primers (needed because DNA polymerase can't bind to single-stranded DNA) to bind (anneal) to the template.
507
PCR Reaction Cycle
1.) Denaturation: Heat to about 95°C. Why: To separate the double-stranded template DNA into single strands so the primers can bind. 2.) Priming (Annealing): Cool to 50-65°C. Why: To allow the short DNA primers (needed because DNA polymerase can't bind to single-stranded DNA) to bind (anneal) to the template. 3.) Elongation (Extension): Heat to 72°C. Why: This is the preferred temperature for Taq DNA polymerase, where the new DNA strands are made. Repeated 35 times
508
Gel electrophoresis
Separates and visualize DNA fragments DNA has a negative charge and therefore moves toward the positive pole. The gel acts as a "molecular sieve," causing small pieces to travel faster and farther.
509
Sanger sequencing
Function: To determine the exact nucleotide sequence of DNA. A PCR reaction is run with the addition of dideoxy nucleotides (ddNTPs). These lack the hydroxyl groups needed for bonding, so when one is incorporated, it terminates elongation. Each ddNTP is tagged with a different fluorescent dye (A, T, C, G).
510
FISH
Fluorescent probes bind specific chromosome regions.
511
RT-PCR
Measures gene expression via reverse transcription + PCR.
512
DNA microarray
Tests gene expression by hybridizing cDNA to thousands of probes.
513
DNA fingerprint
Unique electrophoresis pattern of DNA fragments.
514
Stem Cells
can do mitosis and has the potential to become more than one type of cell. totipotent, pluripotent, or multipotent
515
Totipotent cells
Can become any cell incl. Including embryonic and placental
516
Pluripotent cells
Can become any adult somatic cell. **e.g. embryonic stem cells**
517
Multipotent cells
Can become more than one cell type, usually related types **e.g. blood cells** Adult stem cells tend to be multipotent
518
Nuclear transfer cloning
Adult nucleus into enucleated egg → clone.
519
Recombinant DNA Molecule
A piece of DNA that has parts that come from two different organisms.
520
CRISPR-Cas9
Origin/Why: The system originated as a bacterial "immune system." Allows the cutting and insertion of specific DNA sequences in a living cell. CRISPR is the RNA part that determines where the work is done (the target sequence), and CAS (a nuclease) is the enzyme that does the cutting.
521
Four DNA technology applications
Gene therapy; GM crops; disease diagnosis; forensics; recombinant proteins.
522
Ligand-gated ion channel receptor definition
Receptor in the cell membrane that opens an ion channel when ligand binds.
523
What ligands use ion channel receptors
Water-soluble ligands.
524
Importance of ligand-gated ion channels
Mediate essential functions like nerve signals and muscle contraction.
525
Intracellular receptor location
Cytoplasm or nucleus.
526
What ligands use intracellular receptors
Lipid-soluble ligands that can diffuse through cell membrane
527
Typical intracellular receptor response
Changes in gene expression.
528
Protein kinase function
Adds phosphate group to a protein (phosphorylation), often activating it/leading to amplification
529
Protein kinase role in amplification
One activation can trigger many downstream kinases → amplifies signal.
530
Protein phosphatase function
Removes phosphate groups (dephosphorylation), usually inactivating proteins.
531
Define second messenger
Small, water-soluble molecules that diffuse through cell to relay/amplify signal.
532
Examples of second messengers
cAMP, IP3, DAG, Ca²⁺.
533
How cAMP is formed
ATP with two phosphates removed; phosphate bond position differs from AMP.
534
Calcium ion concentration pattern
Low in cytosol, high in ER.
535
Pathway activating PLC
GPCR activates G protein → activates PLC.
536
What PLC does
Cuts PIP2 into DAG (membrane-bound) and IP3 (diffusible).
537
Role of IP3
Second messenger that opens ligand-gated Ca²⁺ channels on ER.
538
Role of DAG
Membrane-bound portion of PIP2; activates PKC with Ca²⁺.
539
Role of Ca²⁺ in signaling
Triggers events like muscle contraction and nerve function.
540
Transcription factors
Signal to turn on/off for final response
541
Protein activity
signal can have a direct effect on the activity of one or more proteins.
542
Examples of protein activity
Enzyme activation; opening/closing intracellular ion channels.
543
Why single ligand isn’t enough
Cells require multiple receptors activated to trigger full response.
544
Why same ligand has different effects in different cells
Different cells have different relay molecules and pathways.
545
Scaffolding proteins function
Hold enzymes in a pathway adjacent to each other → faster and more accurate signaling.
546
Ways to terminate a signal
Ligand diffuses away Enzymes degrade ligand ligand is endocytosed phosphatases deactivate kinases.
547
Define apoptosis
Programmed cell death.
548
Overall reaction for cellular respiration
C6H12O6 + 6 O2 → 6 CO2 + 6 H2O + Energy (ATP)
549
Type of process cellular respiration is
Catabolic; breaks down glucose to make ATP
550
Major electron carrier molecules
NAD+, FAD, NADP+
551
How many electrons NAD+ carries
2 electrons → NADH
552
How many electrons NADP+ carries
2 electrons → NADPH
553
How many electrons FAD carries
4 electrons → FADH2
554
Location of glycolysis
Cytosol
555
Location of Krebs (TCA) cycle
Mitochondrial matrix
556
Location of oxidative phosphorylation
Inner mitochondrial membrane
557
Is glycolysis aerobic or anaerobic?
Anaerobic
558
Is the Krebs cycle aerobic or anaerobic?
Aerobic
559
Is oxidative phosphorylation aerobic or anaerobic?
Aerobic
560
Is fermentation aerobic or anaerobic?
Anaerobic
561
Net inputs of glycolysis
Glucose, 2 ADP, 2 NAD+
562
Net outputs of glycolysis
2 pyruvate, 2 ATP (net), 2 NADH
563
What must happen before pyruvate enters Krebs?
Converted to acetyl-CoA inside mitochondria; attaches to coenzyme A
564
Net inputs of Krebs cycle (per glucose)
2 acetyl-CoA, NAD+, FAD, ADP
565
Net outputs of Krebs cycle (per glucose)
6 NADH, 2 FADH2, 2 ATP, 4 CO2
566
Complex NADH donates electrons to
Complex I
567
Complex FADH2 donates electrons to
Complex II
568
Types of electron carriers in ETC
Flavoproteins (FMN), Ubiquinone (CoQ), Metal-containing proteins (Cu/Fe/S), Cytochromes
569
Final electron acceptor in aerobic respiration
Oxygen → forms H2O
570
Define chemiosmosis
Using H+ gradient to drive ATP synthesis
571
How ATP synthase works
H+ flows through ATP synthase → rotor spins → ADP + Pi → ATP
572
ATP produced by aerobic respiration
~30–32 ATP per glucose
573
ATP produced by anaerobic fermentation
2 ATP per glucose
574
What fermentation is
Incomplete oxidation; regenerates NAD+ so glycolysis can continue
575
Products of fermentation
Acids or alcohols + CO2
576
How fermentation connects to glycolysis
Regenerates NAD+ for glycolysis
577
Define acidic fermentation
Fermentation producing organic acids (e.g., lactic acid)
578
Define homolactic fermentation
Pyruvate → lactic acid only
579
Define alcoholic fermentation
Pyruvate → ethanol + CO2
580
Organisms that do alcoholic fermentation
Yeast
581
How lipids provide energy
Glycerol + fatty acids enter glycolysis/Krebs
582
How proteins provide energy
Amino acids deaminated → enter Krebs