Topic 2: Molecular Biology Flashcards

1
Q

molecular biology

A

explains living processes in terms of the chemical substances involved

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2
Q

Discover of DNA

A

1953

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3
Q

Nucleic acid

A

large biomolecules (DNA & RNA)

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4
Q

Urea

A

compound produced by living organisms but can also be synthesised.
- animals synthesis to remove excess nitrogenous waste from excess amino acids

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5
Q

Process of urea synthetisation

A

synthesised in the liver, then filtered out of the blood by the kidneys and excreted in the urine.

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6
Q

urea chemical equation

A

CO2(HN)2

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7
Q

Chemical equation of artificial urea

A

ammonia + carbon dioxide -> ammonium carbonate -> urea + water

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8
Q

falsification of vitalism

A

artificial synthesis of urea falsified vitalism

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9
Q

Vitalism

A

Only organisms can synthesis organic compounds

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10
Q

atom

A

are the basic unit of all matter

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11
Q

elements

A

substances made up of only one type atom

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12
Q

molecules

A

two or more atoms are held together by chemical bonds

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13
Q

Organic compounds

A

organisms containing these primarily have hydrogen and carbon

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14
Q

covalent bonding

A

sharing electrons between two molecules to achieve stablity

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15
Q

ionic bonding

A

attraction, one molecule take an electron from another. one molecules is positive (cation), and one is negative (anion)

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16
Q

Carbohydrates

A

most abundant organic molecules.
- are a chemical energy source
- form structural components
-form parts of DNA and RNA
-Combine with proteins to form glycoproteins and glycolipids.

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17
Q

Breaking Saccharides

A

Polysaccharides and disaccharides can be broken down into smaller molecules via hydrolysis

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18
Q

Hydrolysis

A

the splitting of the molecules with water

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19
Q

Glucose

A

involved with energy production in cell respiration
polar
carried by blood in the plasma

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20
Q

Fructose

A

a component of flower nectar to attract pollinators

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21
Q

Sucrose

A

the transport form of carbohydrates in plants (phloem)

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22
Q

Glycogen

A

storage in liver

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23
Q

Cellulose

A

the storage form of glucose found in the cell wall.

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24
Q

Examples of monosaccharides

A

Glucose, Galactose, and fructose

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25
Examples of disaccharides
Maltose, Lactose and Sucrose
26
Examples of Polysaccharides
Glycogen and Cellulose
27
Proteins
large organic compounds made of amino acids arranged into one or more linear chains
28
Enzyme Proteins
Acceleration of chemical reactions
29
Transport Proteins
Transportation of substances
30
Structural Proteins
Support
31
Hormonal Proteins
Chemical communication with an organism
32
Receptor Proteins
Response of a cell to chemical messages
33
Motor Proteins
Movement
34
Defensive Proteins
Protection against disease
35
Nucleic acids
Chain of sub units called nucleotides
36
Simple Lipids
Includes Fat, Steroids and hormones, composed of Fatty Acid and Glycerol.
37
Fatty acids
can be saturated or unsaturated
38
Saturated Fat
Contained the maximum number of hydrogens with no double carbon bonds.
39
Unsaturated Fats
Must contain at least one double carbon bond
40
Anabolic reaction
builds molecules
41
Catabolic molecules
break down molecules
42
Anabolism
synthesis of complex molecules from simpler molecules
43
maltose synthase
condenses two molecules of glucose into maltose forming a glyosidic bond
44
Ribosomes in anabolism
Condeses two amino acids into a dipeptide forming a peptide bond.
45
Protease hydrolyses
a dipeptide into two amino acids breaking the peptide bond
46
Lactose Hydrolyse
Lactose into glucose and galactose breaking the glyosidic bond
47
Cohesion (water)
- bonds present = tetrahedral, give cohesive force and increase strength - strongly cohesive tend to stick to one another
48
Adhesion (water)
Attract to other polar molecules
49
Solvent (water)
- Polar attraction of large quantities of water molecules can interrupt intra-molecular forces and result in the dissociation of the atoms
50
Hydrophilic
substance attracted to water substance that dissolves and adheres to water.
51
Hydrophobic
non-polar all lipids like dissloves like
52
amino acids
positive and negative chargers - R group determines polarity and t/f solubility carried by the blood plasma
53
oxygen
non polar soluble as temp increases, solubility decreases at 37 degrees, little oxygen can be carried by the plasma. haemoglobin in the red blood cells carry most oxygen
54
Fats (transport)
Non polar molecules carried in blood inside lipoproteins complexs
55
Cholesterol (MB)
hydrophobic, apart from small hydrophilic part carried in blood in lipoprotein complexes
56
Lipoprotein complexes
- outer layer of phospholipid molecules - hydrophilic phosphate heads face outwards, connect with water - hydrophobic hydrocarbon tails face inwards connecting with fats - cholesterol molecules are positions in the phospholipid monolayer.
57
Sodium Chloride
- ionic compound -freely soluble in water -carried in the blood plasma
58
Thermal (water)
- high specific heat capcity (4.2 joules is required to increased temp by 1) High heat of vaporisation and fusion B/c hydrogen bonds need to be broken.
59
Water as a coolant
increased temp damages tissues and denatures proteins takes energy to change temperature when water evaporates, removes energy from the system. felt as cooling b/c excess heat energy is removed from the body. Skin and blood vessels are cooled.
60
difference between water and methane
water =polar methane = non polar
61
methane (MB)
- waste product of aerobic respiration in certain prokaryotes - can be used in fuel - contributes to the greenhouse effect
62
Methanogenic Prokaryotes
- found in swamps, wetlands, and the guts of animals - found in waste dumps
63
monosaccharides examples
Glucose, Galactose, Fructose, Ribose
64
Disaccharides examples
Maltose, Lactose, Sucrose
65
Poly Sacchardies example
Cellulose, Amylose and Amylopectin, Gloceryn
66
Functions of Lipids
1- Energy storage 2- Subcatenos fat as a buoyancy aid and thermal insulation 3- Water proofing of hair and feather 4- Electrical conductivity
67
Energy Storage
mass for mass lipids produce more energy than carbohydrates
68
Water proofing of hair and feahters
Oil secretions from sebaceous glands in mammals and preen glands in birds preventing water logging and increase efficency of movement.
69
Electrical conductivity
myelin lipids of Schwann cells are involved in neurosignal transduction.
70
Cis-ismoers properties
- common -double bond becomes bend in a fatty acid chain -loosely packed -triglycerdies formed typically liquid at room tempature
71
TRans-simoers
-Rare -double bond doesn't bend -closely packed -trigyclerins are typically soild at room tempature.
72
Draw the amino acid strucutre
73
fibrous protein properties
-long and narrow -structural -insouble in water -repetitive amino acid -less sensitive to change in temp, PH
74
Globular proteins
-round/spherical - functional -soluble in water -irregular amino acids -more senstive to change
75
Protein uses: CAtalysis
there are thousands of different enzymes to catalyse specific chemical reactions within or outside a cell
76
protein uses: Muscle contraction
actin and myosin together cause the muscle contraction used in locomotion and transport around the body
77
Protein uses: Cytoskeletons
tubulin is the subunit of microtubules that give animals cells their shape and pull on chromsones during mitosis
78
Protein uses: Tensile strength:
Fibrous proteins give tensile strength needed in skin, tendons, ligaments and blood vessel wall
79
Protein uses: Blood clotting
plasma proteins act as clotting factors that cause blood to turn from a liquid to a gel in wounds
80
Protein uses: Transport of nutrients and Gases
Proteins in blood help transport oxygen, carbon dioxide, iron and lipids
81
Protein uses: Cell adhesion
membrane proteins cause adajacent animals cells to stick to each other within tissues
82
Protein uses: Membrane transport
Membrane proteins are used for facilitated diffusion and active transport, during cell respiration and photosynthesis
83
Protein uses: Hormones
some such as insulin, FSh and LH are protein but hormones are chemically diverse
84
Protein uses: Receptors
Binding sits in membrane and cytoplasm for hormones, neurotransmitters, taste and smells and also receptors for light in the eye and in plant.
85
Protein uses: Packing of DNA
Histones are associated with DNA in eukaryotes and help chromosomes to condense during mitosis
86
Protein uses: Immunity
This is the most diverse group of proteins as cells can make huge numbers of different antibodies
87
Rubisco
Enzyme- catalyses the reaction that fixes carbon dioxide in the atmosphere. -provides carbon for most organisms.
88
Insulin
hormone- signals many cells to absorb glucose and help reduce the glucose concentration of the blood
89
Immunglobins
two antigen binding sites - a molecules on the pathogen which invokes a immune response
90
Rhodopsin
-pigment that absorbs light -membrane protein of rod cell of the retina -consists of the opsin polypeptide surrounding the retinal prosthetic group.
91
Collagen
- rope like proteins made of three polypeptides wound togehter -1/4 of protein in human body is collagen -forms a mesh of fibres in skin and in blood vessel walls that resists tearing
92
spider silk
different silk=different functions dragline silk is strogner than steel and tougher than kelvar - when first made it contains regions where the polypeptide forms parallel arrays and some regions resemble a distored tangle -when stretched the poypeptide extends make the silk extensible and resistant to breakage
93
genome
all of the genes of a cell, a tissue or an organism
94
Proteome
all of the proteins produced by a cell, tissue or an organism
95
Denaturation of protein
ITs irrevisble and caused by heat, extreme ph condtions
96
Denatuation of proteins: Heat
heat can cause denaturation: vibrations within the molecule breaks intramolecular bond or intereactions.
97
Denaturation of proteins: PH
extremes of ph: charges on R group are changed bresking ionic bonds within the protein or causing new ionic bonds to form.
98
Metabolism functions
overall chemical activity of your cells - synthesising biomolecules -energy formation and transformation -recycling materials -breaking down unwanted materials
99
Enzymes
-Proteins -Substrate specific -Reusable -Effective in small amounts -Reduce the activation energy of a reaction -able to catalyse the reaction both ways -not able to change the direction of the reaction -not able to change the final amount of the reaction
100
Enzyme activity
enzyme catalysis involves molecular motion and the collision of substrate with the active site.
101
Three stages of enzyme activity
1. The substrate bind to the active site of the enzyme (this forms the enzyme-substrate complex) 2. Chemical bonds in the substrates are stressed and new bonds form between substrate molecules (or bonds in a large substrate are broken) 3. the products seperate from the active site, leaving it vacant to catalyse another reaction
102
Collision theory
a reaction will only happen if the particles have the correct orientation and enough energy
103
Factors affecting enzyme activity
-tempature -pH -inhibtion amount of reactant coenzymes and cofactors
104
Temperature (enzyme activity)
adding heat increases enzyme reactions as the molecules are moving around faster and colliding more often. too much heat can damage the structure of the enzymes and denature the enzyme.
105
pH (enzyme activity)
shape of proteins can be affected by pH, altering the fit between the enzyme and the substrate pH is a measure of hydrogen ions. Enzymes shape is often created with hydrogen bonds.
106
Substrate and product concentration (enzyme activity)
increasing the concentration of the substrate will increase the amount of reactions until the enzyme becomes saturated, adding more enzymes will fix this.,
107
how lactose free milk is made
1. make the enzyme lactase with bacteria. insert the gene that codes for the enzyme into the genome of a bacteria plasmid and let the bacteria create the enzyme vis protein synthesis 2. immobilise the enzyme and combine with the milk, enzymes are held in place via entrapment. milk is then passed through these enzymes and the lactose is converted into lactase.
108
immbolized enzymes
have been attached to other materials or included in aggregation so that the movement of the enzyme is restricted
109
immbolisation of enzyme techniques
-attaching enzymes to a glass surface -trapping enzymes in alginate gel -bonding enzymes together to form aggregates
110
Advantages of immobilized enzymes
- the enzymes can be separated from the solution containing products of the reaction, stopping the reaction when needed. -enzyme can be retrieved and reused -immobilization increased the stability of the enzyme to changes in temp and pH -higher enzyme concentration can be used, increasing the rate of reactions.
111
chloroplast structure
membranous structure: outer and inner membrane, plus thylakoid structure composed of membrane. Fluid filled Enzymes needed for photosynthesis reactions located in the fluid matrix (stroma) usually twice as long as wide
112
Draw a chloroplast diagram
look at book
113
photosynthesis
energy conversion, as light energy is converted into chemical energy in carbon compounds
114
carbohydrate at the end of photosynthesis
3-carbon molecule glyceraldehyde-3-phosphate, G3P this is converted into glucose and also used to make fatty acids and amino acids.
115
draw the G3P diagram
check diagram
116
ATP equation
two phases, first aborbing and converting the required energy to chemical energy. then the second phase. equation: carbon dioxide+ water -> carbohydrate +oxygen
117
light dependent reactions
occur within thylakoid membranes, chlorophyll absorbs light energy, light energy converted to ATP and NADPH. energy sources for light independent reactions, water is the source of hydrogen required for glucose.
118
light independent reactions
occur in fluid filled stroma, the reactions are endergonic and use ATP and NADPH previously produced ADP- low energy form of ATP NADP+ = low energy form of NADPH can be recycled to produce original form
119
photolysis
light energy is used to split a water molecule to release hydrogen ions needed later, oxygen is surplus and diffused out
120
photolysis of water equation
2H20 > 4e- + 4H+ + O2 for 2 molecules of water, half for one molecule
121
effects of photosynthesis on earth
--increase in photosyntheic organisms and the accumulation of oxygen in the atmosphere became measure about 2.4 billion years ago and rose to 2% ( this is known as the great oxidation event) 2.2 billion years ago which it stayed until 750 million years ago. oxygen in the atmosphere decreases the methane concentration and photosynthesising organisms use up carbon dioxide. increases oxygen in atmosphere lead to increase in ocean, caused oxidation of dissolved iron in the water and the iron oxide precipitate feel onto the sea floor forming bands of iron oxide. the atmosphere since 750mya has risen to 20.05% oxygen concentration.
122
limiting factors of photosynthesis
temperature, light intensity, and carbon dioxide concentration
123
Light intensity (photosynthesis)
-as light intensity increases, more energy is avaliable and the rate of photosynthesis increases. -this is a straight increase until reaching a plateau in which no further increase in co2 consumption can occur, as the light intensity cannot support the rate of reaction.
124
temperature (photosynthesis)
rising: increasing molecular collisions due to increased kinetic energy lrads to an increase in the rate of photosynthesis. tip: maximum rate of photosynthesis reached at the optimal temperature too high: breaking of bond in enzymes structure leads a change in shape of the active site (denaturation) decreasing the rate of photosynthesis -shape is a bell curve for graph.
125
carbon dioxide concentration
positive correlation, until rate of photosynthesis reaches a plateau (plants reach saturation level with CO2) no further increase unless temperature or light intensity is increases, o possibly too little CO2 due to amount of photosynthetic organisms.
126
when is visible detectable
from 400 to 700 nanometers
127
wavelengths of light
red to violet, red = longest wavelength gamma rays - long radio waves shorter = higher energy, lower frequency = lower energy
128
what light does chlorophyll absorbs
-red and blue light, and reflects green light. white or transparent substances don't absorb light.
129
two types of nucleic acids
dna: deoxyribonucleic acid rna: ribonucleic acid
130
draw a nucleotide
-pentose sugar, phosphate group and nitrogenous base
131
difference between rna and dna (molecularly)
carbon two dna: only hydrogen comming off rna: hydroxide coming off c2
132
difference between DNA and RNA
- dna: double stranded rna: single stranded -dna: thymine rna: uracil dna: deoxyribose sugar rna: ribose sugar
133
base pairings
adenine (b) - thymine or uracil - 2 lines cytosine- guanine (b) - lines
134
purines
adenine and guanine
135
pyrimidines
cytosine, thymine and uracil
136
draw dna
label 3' and 5' carbon corners, oppisite on both sides
137
what type of bonding is used for nitrogenous bases
hydrogen bonding
138
discovering the structure of dna
Crick and watson, used model-making to discover the structure of dna.
139
DNA replication
the purpose of dna replication is to produce two identical copies of a dna molecule. essential for cell growth or repairable of damaged tissue. ENSURES THAT EACH NEW CELL RECIEVES ITS OWN COPY OF THE DNA
140
dna helicase
DNA helicase separates the two polynucleotides strands of DNA by breaking the hydrogen bonds between complementary base pairs -is required to unwind and unzip the DNA double helix.
141
Dna polymerase
links nucelotides together to form a new strand, using pre-existing strand as a template. only copies from5' to 3' -catalyses the formation of a new DNA strand that is complementary in sequence to the original DNA template strand. -DNA polymerase brings a nucleotide into a position where its base can form hydrogen bonds with the complementary base on the template strand, then catalyses a covalent bond between that nucleotide and the one before it in the new, growing DNA strand.
142
stages in DNA replication
stage one: helicase unwinds the double helix and separates the two strands by breaking hydrogen bonds 2: DNA polymerase links nucleotides together to form new strands using the pre-existing strands as templates. completes from 3' to 5', which is the template. new build goes from 5' to 3' 3: the daughter DNA molecule each rewind into a double helix
143
semi conservative replication of DNA
each strand contains one original and one new strand. this is its own model
144
conservative model
an entirely new molecule is synthesised from a DNA template (which remains unaltered
145
semi conservative model
each new molecule consists of one newly synsthesised strand and one template strand
146
dispersive model
new molecules are made of segments of new and old DNA
147
Three types of RNA
mRNA Rrna tRNA
148
mRNA
serves as a temporary copy of DNA and carries the DNA codes from the nucelus to the ribosome
149
rRNA
ribosomal rna makes up the ribosome
150
tRNA
transfer RNA carries a specific amino acid to the ribosome and adds it to the growing polypeptide
151
limitations of DNA polymerase
- can not start the attachment process, as it needs a primer or is done by RNA
152
PCR
-the polymerase chain reaction -use of Taq polymerase to produce multiple copies of DNS, rapidly by chain reaction. --this polymerase is obtained from a bacterium, thermus aquaticus, that lives in hot springs. -has to be heat stable to prevent denaturation. can t/f resist the brief period of the cycle where the temp = 95, to separate DNA strands.
153
PCR method
1: denaturation -at 95 for 15 seconds -double stranded DNA seperates to form two new strands. 2: attaching primer (annealing) - at 54 for 25 seconsd primers attach to complementary sequences, so that Taq DNA polymerase can add nucelotides. 3: elongation (extending primers) at 72 for 80 seconds, allows all single stranded DNA to be copied. 72 is the optimal tempature/ taq DNA polymerase forms a complementary strand for each template strand.
154
stages in DNA polymerase
1: A nucleotide with the correct base is brought in by DNA polymerase. 2:Hydrogen bonds form between complementary bases. 3:DNA polymerase catalyses a covalent bond between the 5’ terminal of the new nucleotide and the 3’ terminal of the previous nucleotide. 4:DNA polymerase moves to the next nucleotide on the template strand and repeats step 1-3.
155
stages in DNA polymerase
1: A nucleotide with the correct base is brought in by DNA polymerase. 2:Hydrogen bonds form between complementary bases. 3:DNA polymerase catalyses a covalent bond between the 5’ terminal of the new nucleotide and the 3’ terminal of the previous nucleotide. 4:DNA polymerase moves to the next nucleotide on the template strand and repeats step 1-3.
156
evidence for the theory of semi-conservative replication
-1958, Mathew Meselson and Franklin Stahl developed a methodology to investigate DNA replication, was possible in part to to Harold Uery's work in purifying stable isotopes for use in tracing biochemical pathways/ two isotopes of nitrogen (normal N14, and rare N15)
157
evidence for the theory of semi-conservative replication
-1958, Mathew Meselson and Franklin Stahl developed a methodology to investigate DNA replication, was possible in part to to Harold Uery's work in purifying stable isotopes for use in tracing biochemical pathways/ two isotopes of nitrogen (normal N14, and rare N15) - the caesium chloride solution is centrifuged, the dense caesium ions move towards the bottom of the tubes. -carsium ions fo not sediment fully b/c of diffusion, a concentration gradient is established. these substances become concentrated . corresponding to density.
158
Meselson and Stahl's experiment.
-cultured e'coli, bacteria in a medium containing 15^N. the results concluded that all the nitrogen atoms in the DNA had denser 15^N. bacterial was then tranffered to a medium of 14^N. DNS samples were collected at regular time intervals for several hours, allowing for replication of DNS over four generations.
159
Analysis of Meselson and Stahl's results
- demonstrated that DNA replicated semi-conservatively , meaning that each strand serves as a template for synthesis of a new, complementary strand. -although experimented in bacteria, we know that DNA replication is a universal mechanism.
160
Gene expression
process by which information from a gene is used in the synthesis of a functional gene product. The process of gene expression consists of two phases: -Transcription, where a gene sequence is read by RNA polymerase and used to build a complementary strand of RNA -Translation, where the RNA strand, called messenger RNA (mRNA), is read by a ribosome and used to determine the amino acid sequence of a new polypeptide
161
Transcription
-the synthesis of mRNA copied from the DNA base sequences by RNA polymerase. -* The strand that is transcribed is called the antisense strand and is complementary to the RNA sequence * The strand that is not transcribed is called the sense strand and is identical to the RNA sequence (with T instead of U)
162
Steps of Transcription
1. RNA polymerase separates the DNA strands and synthesizes a complementary RNA copy from one of the DNA strands 2. When the DNA strands are separated, ribonucleotide triphosphates align opposite their exposed complementary base partner 3. RNA polymerase removes the additional phosphate groups and uses the energy from this cleavage the covalently join the nucleotide to the growing sequence 4. Once the RNA sequence has been synthesised, RNA polymerase detaches from the DNA molecule and the double helix reforms.
163
translation
* Translation is the process of converting a sequence of mRNA nucleotides to a sequence of amino acids * This process occurs in the cytoplasm and results in a polypeptide chain (protein)
164
triplets
group of three letters of DNA
165
codon
-three letters of mRNA
166
anticodons
compeltmentary to codons on tRNA
167
Steps of translation
1. mRNA binds to a ribosome 2. A tRNA molecule with an anticodon that is complementary to the codon on mRNA binds to the mRNA 3. Another tRNA with an anticodon complementary to the second mRNA codon attaches to the mRNA molecule at the ribosome 4. An enzyme joins the two amino acids on the tRNA molecules together via a condensation reaction 5. The bond is broken between the tRNA molecule and the amino acid that was just added to the polypeptide chain 6. The tRNA molecule is released 7. The ribosome moves down to the next mRNA codon 8. This process is repeated many times to form the amino acid chain
168
genetic code
-said to be universal -because the same triplets make the same codons which are translated into the same amino acids in ebery single organism on earth
169
what is ATP
adenosine triphosphate -a high energy molecule that functions as an immediate source of power for cell processes.
170
use of ATP
o Synthesis of macromolecules. This include DNA, RNA and proteins o Active transport o All movements in the cell, such as muscle contraction, endocytosis, exocytosis, etc
171
anaerobic respiration
-oxygen not present -glucose only -yield of ATP per glucose per small products: Humans: Lactate Yeast: CO2 and ethanol
172
aerobic respiration
-oxygen present -substrate is glucose or lipids large atp yield products: CO2 and water
173
CO2 and baking
* Yeast is used in baking bread. It is mixed into the dough before baking * The yeast rapidly uses up all oxygen present in the dough and then produces ethanol and carbon dioxide by anaerobic cell respiration. The carbon dioxide forms bubbles making the dough rise * It increases the volume of the bread and makes it less dense. When the dough is based most of the ethanol evaporates and the carbon dioxide bubbles give the bread a light texture
174
Ethanol and brewing and biofuel industries.
* Yeast can be used to produce ethanol by fermentation. The yeast is cultured in a liquid containing sugar and other nutrients, but not oxygen so its respires anaerobically * The ethanol concentration of the fluid around the yeast cells can rise to approximately 15% by volume, before it becomes toxic to the yeast and the fermentation ends. Most of the carbon dioxide bubbles out into the atmosphere * Beer, wine and other alcoholic drinks are brewed in this way * Ethanol is also produced by fermentation for use as a fuel
175
Glycolysis
-all celluar respiration pathways begin with glycolysis anaebroic process
176
process of glycolysis
1. Starts with glucose (6 carbons) 2. An enzyme modifies to make it unstable 3. A series of reactions splits the glucose into 2 molecules of pyruvate (3 carbons each) 4. The energy from the bond that are broken in this process are used to generate 2 ATP molecules * To make the glucose unstable 2 ATP molecules are needed. The breaking of glucose generates 4 ATP molecules * So, we say that 2 ATP molecules are spent, 4 are generated, and that results in a net gain of 2 ATP molecules
177
fermentations
-after glycolysis if no oxygen, organisms undergo fermentation. -The breakdown of organic molecules for ATP production anaerobically * Fermentation also takes place in the cytoplasm as it is anaerobic
178
alcoholic fermentation
Example Organism: Yeast 1. Starts with pyruvate 2. Ends with alcohol and carbon dioxide Real World Application: Yeast fermentation is sued to produce bread, beer and wine
179
lactic acid fermentation
Example Organisms: Bacteria, Animals 1. Starts with pyruvate 2. Ends with lactic acid Real World Application: Production of sour cream, yogurt, cheese, and muscle soreness after exercise in animals
180
aerobic respiration
when oxygen is present organisms undergo aerobic respiration in the mitocondria.