Topic 2 & Some Topic 7: Molecular Biology Flashcards

DP2- U1: Biochem

1
Q

A. Chemical Elements and Water

1.define molecular biology

A

the study of living processes in terms of the chemical substances

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2
Q

A. Chemical Elements and Water

2.contrast the synthesis of urea in the body and artificially.

i.what urea +ii. body/transportation/path+iii. why artifical/steps/path

A

i.
urea is produced in our body as a way of excreating nitrogen from excess amino acids
ii.
- synthesized in the liver and uses enzymes.
- urea to blood stream to kidneys to filtered and released by urine.
- cyclic chemical pathway and complex
iii.
- artifical is done to help produce millions of tons of nitrogen fertilizers for crops
- 2 main steps & does not use enzymes + is identical to normal urea
- linear and simple

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3
Q

A. Chemical Elements and Water

3.Outline how the artificial synthesis of urea lead to the falsification of theories.

i.what is the theory/meaning ii. Who and how did they falsify it

A

i.
- Vitalism theory: the orgin and phenomena of life are due to a vital principle which is different from purely chemical or physical forces. Organic compounds in plants/animals could only be made with the help of a vital principal
ii.
Wöhler accidentally falsified this theory by artifically synthesizing urea in 1828 when trying to prepare ammonium cynate. Since Wöhler created urea it undermined the theory of needing a vital force to create an organic compound.

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4
Q

A. Chemical Elements and Water

4.Explain how the chemical properties of carbon allows for a diversity of compounds.

i.type/strength of bond ii.form how many bonds? and example

A

i.
- form covalent bonds
- strongest intramolecular force because they evenly share electrons. thus, no confilict to weaken the arrangement.
ii.
- contains 4 electrons in valence shell allowing them to form 4 covalent single bonds with other potential elements.
ex. methane= CH4

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5
Q

A. Chemical Elements and water

5.Outline the four classes of carbon compounds

i. elements in each class ii. made of/properties iii.examples or use

A

a. Carbs
i. (C, H, O)
ii. 1 or more simple sugars (monomers). Many monomers make monosacchride which make polysacchrides
iii. startch, cellulose, glycogen

b. Lipids
i. (C, H, O)
ii. insoluble in water, soluble in nonpolar organic solvents
iii. triglycerides (fats, oils), phospholipids, steriords

c. Protiens
i. (C, H, O, N) sometimes sulphur
ii. large organic compounds made up of amino acids
iii. use protiens for hormones, enzymes, gas transport etc.

d. Nucleic Acids
i. (C, H, O, N, P)
ii. covalently bonded sugars (ribose= RNA, deoxyribose= DNA) , phosphates, and bases to form nucleotides which are what the chains are made up of.
iii. RNA and DNA

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6
Q

A. Chemical Elements and water

10.Explain Water Polairity

what is polarity/how is water polar

A

water is polar because the covalent bond formed between the oxygen molecule and two hydrogen molecules exhbit an unequal share of electrons and unsymmetrical shape. This in turn creates two poles in the molecule; one being partialy negative (oxygen) and one being partially positive (hydrogen). This unequal share of electrons then makes the molecule polar and is also known as a dipole.
These dipoles attract other polar compounds and H2O molecules associate via hydrogen bonding between the H and O areas on many molecules.

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7
Q

A. Chemical Elements and water

12.Outline the four properties of water giving an example of each

and how the property is formed

A

1. Cohesion
defn: water sticking to water because of close attraction forming a tight sticky pack
how: the polairty and electronegativity difference of water
ex: A simple example of cohesion in action comes from the water strider (below), an insect that relies on surface tension to stay afloat on the surface of water.

2. Adhesive
defn: water sticking to polar surfaces
how: same reason they stick to themselves- polairty, h-bonds, delta electronegativity
ex: Capillary action- able to adhere H2O molecules to the polar surface of the xylem cellulose vessel. also ex of cohesion since the water molecules are sticking to themselves.

3. Thermal
defn: relating to changing the state or temp of water by energy (usually heat). Heat capacity of water is 4.186 J/g ºC= that much energy needed to heat a gram of water by 1ºC
how: stength of h-bonds allows for a lot of energy needed to change the state/temp of water. Causes water to heat or cool more slowly than other substances.
ex: stable internal enviroment for all living things because water cant change temp too easily. (humans are made up of 70% water)

4. Solvent
defn: water being able to dissolve other polar substances.
how: waters polarity (large amounts) allows it to interupt intramolecular forces allowing it to dissociate atoms. reason it is a great solvent
ex: salt & water; Na+ is surrounded by O- regions whereas Cl- is surrounded by H+ regions allowing the crystal lattice to dissociate and pull apart.**

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8
Q

A. Chemical Elements and water

13.Contrast hydrophilic and hydrophobic

add examples

A

hydrophilic: polar or charged substances that are chemically attracted to water. Can dissolve in H2O. ex. glucose, sodium and chlorine ions, cellulose surfaces

hydrophobic: non-polar and uncharged substances that are chemically unattracted to water. cant dissolve in H2O. ex. fats, oils, alcohols

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9
Q

A. Chemical Elements and water

14.Compare the thermal properties of water and methane.

only need to memorize two for each molecule

A

methane
formula: CH4
Polarity: non-polar
density gm c-3 :0.46
specific heat capacity Jg-1ºc-1: 2.2
Latent heat of vapourisation J g-1: 510
melting point ºC: -182
boiling point ºC: -161.6

water
formula: H2O
Polarity: polar
density gm c-3: 1
specific heat capacity Jg-1ºc-1: 4.18
Latent heat of vapourisation J g-1: 2240
melting point ºC: 0
boiling point ºC: 100

Latent heat of vapourisation: energy from liquid to gas

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10
Q

A. Chemical Elements and Water

15.Outline the use of water as a coolant in sweat.

what property of water states water is a good coolent+ expectation

A

Water’s thermal property mentions how 1g of water must absorb 4.18 Jg-1ºC of heat before the temperature is inceased by 1ºC (SHC). thus, water is a good coolant as it can absorb heat easily but changes its temp slowly.
in order for humans to maintain a stable internal heat temp of 37ºC, when we are overheating, we sweat. sweat is made up of 99% of water so it can absorb the heat easily and simply be removed. #homeostasis

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11
Q

A. Chemical Elements and water

16.Outline the transport of sodium chloride, amino acids, glucose, oxygen, fat molecules and cholesterol.

i. solubility in water/ ii. how is it carried in the blood

A

Glucose:
i. polar thus soluble
ii. blood plasma (consists of 95% water and other substances which are transported)

Amino acids:
i. polar because of amine and acid groups + negative and positive charges. even if the R-groups are nonpolar it just effects the degree of solubility.
ii. blood plasma

sodium chloride:
i. ionic compound thus polar and soluble. dissolves to form Na+ and Cl- ions
ii. blood plasma

Oxygen:
i. nonpolar but due to small size it is soluble in water. as the H2O temp goes up the solubility of oxygen decreases.
ii. hemoglobin in red blood cells carries the majority of oxygen. 4 binding sites of oxygen. at normal body temp very little oxygen can be carried by the plasma.

cholestrol:
i. insoluble- mainky hydrophobic except for head. too small to be significant.
ii. carried in the blood plasma by lipoprotiens.

fats:
i. insoluble- large non-polar molecules
ii. blood plasma by lipoprotiens

lipoprotiens: outer layer of phospholipds hydrophilic heads out and hydrophobic tales inside. Hydrophobic ends in contact with non-polar end of cholestrols, fats and protiens.

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12
Q

A. Chemical Elements and water

17.Explain (with examples) how disaccharides and polysaccharides can be formed from monosaccharide monomers.

be able to draw it

A

glucose + glucose → maltose + water
glucose= monomer
maltose= disaccharide
→= condensation reaction (when water product is formed from each of the reactants)

the hydrogen attached to Carbon-1 on one glucose molecule and the HO group attached to Carbon-4 on another glucose molecule dissociate by an enzyme to form water product.
maltose is formed by creating a glycosidic bond (covalent bond with oxygen in the middle) between carbon-1 and carbon-4. This oxygen comes from the OH molecule attached to carbon-1 on the same molecule that gave up the hydrogen from carbon-1 (removed by enzyme).

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13
Q

B. Carbohydrates & Lipids

18.Use visualization software (i.e. Jmol) to compare cellulose, starch and glycogen.

compare the structure of these molecules with glucose/fructose/sucrose

A

look at other document with drawings

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14
Q

B. Carbohydrates & Lipids

19.Compare the structure and function of the polysaccharides cellulose, starch and glycogen.

A

Cellulose
structure: 1-4 bonds of beta glucose molecules. straight (chain as each subunit flips) and unbranched.
function: used in cell walls and prevents plants from bursting under high tugor pressure. high tensile strength due to H-bonds, insoluble in water.

Startch
function: useful for glucose and energy storage in plants. stored temporarly in leafs when more glucose is made than for transport. insoluble, easy to add and remove glucose units.
Amylose:
structure: 1-4 bonds of alpha glucose molecules. straight and unbranched chain, forms a helix shape.
Amylopectin
structure: 1-4 and 1-6 glycosidic bonds of alpha glucose molecules. bent and branched, forms a globular shape.

Glycogen
structure: 1-4 and many 1-6 bonds of alpha glucose. bent and branched chain, forms a compact shape.
function: useful for glucose and energy storage, stored in live and human muscles, used in cells where large amounts of glucose storage would cause a problem. insoluble, easy to add and remove glucose subunits. made by animals and some fungi.

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15
Q

B. Carbohydrates & Lipids

20.Compare lipids to carbohydrates to determine which is more suitable for long term energy storage in humans.

2 reasons why. also mention glycogens role.

A

lipids are better for long term energy storage because:
1. the amount of energy released in cell respiration per gram of lipids is double that for carbs/protiens
2. Lipids add 1/6 as much to body mass as carbs thus fats are stored as pure droplets whereas 1g of glycogen (stored form of glucose-carb) is stored and associated with 2g of water— essential for active animals.
- fats are for energy storage: the energy is stored in speacilized groups of cells called adipose tissues located beneath the skin and around kidneys/ other organs

Glycogen is used for medium term storage:
glycogen is stored energy in the liver and muscles that is more readily avaliable than the energy stored in fats. Thus its good for quicker usage/short-medium term storage.

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16
Q

B. Carbohydrates & Lipids

21.Determine body mass index by calculation or use of a nomogram.

what is it and what is the formula

A

BMI used to identify weight problems- not a diagnostic tool.

BMI= mass in kg/(height in meters)^2

BMI unit= kg m^-2
nomogram: picture where you use a ruler to draw a line between height and weight to see the BMI

BMI vs status table will be given

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17
Q

B. Carbohydrates & Lipids

22 Outline the (2) types of fatty acids

Saturated?uns:structure/hydrogen/natural or synthesized/shape/density

A

Saturated:
refers to if more hydrogen atoms can be added to a fatty acid. a saturated fatty acid can’t add anymore hydrogens. an unsaturated fatty acid can add more hydrogens by getting rid of a double bond and replacing it with hydrogen.

Unsaturated
Cis-isomers
structure/positioning of hydrogen: C–C double bond with hydrogens on same side
natural or synthesized: common in nature
shape: all hydrogens on one side make it bent
density: loosley packed as its bent

Trans-isomers
structure/positioning of hydrogen: C–C double bond with hydrogens on opposite side
natural or synthesized: rare in nature- usually artificially produced
shape: linear- balance of hydrogen on either side
density: closley packed because linear

saturated= no double bonds
monounsaturated= 1 double bond
polyunsaturated= greater than one double bond

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18
Q

B. Carbohydrates & Lipids

23.Explain the process and component parts from which triglycerides are formed.

also know how to annotate it

A

A glycerol molecule and three fatty acids go through a condensation reaction. Three OH compounds are taken from the glycerol molecule, and one hydrogen atom is seperated from each OH compound on all of the fatty acids (3). Those react to form the product of 3 H2O. The oxygens left over on the fatty acids then bond with the carbon on the glycerol molecule. This is called an ester bond.

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19
Q

B. Carbohydrates & Lipids

24.Outline the evidence related to the health risks of trans-fats and saturated fats.

main concern + cause/effect & evidence for and against (1 for latter)

A

main concern: Coronary heart disease (CHD)
causes: saturated and trans fats. also dietary fibre and genetic factors
effects: coronary arteries become partially blocked by fatty deposits (atherosclerosis) leading to blood clot formation and heart attacks.

evidence for CHD being caused by trans and saturated fats:
1. CHD is rarely seen in countries near the meditararian where diets rich in olive oil are consumed. olive oil contain cis-monounsaturated fatty acids.
2. Trans-fats correlate with CHD. patients who had died from CHD had trans fats in the fatty deposits in the diseased arteries. causal link. also trans fats mimic saturated fat structure- thus they are also correlated with CHD

Not evidence for CHD being caused by trans and saturated fats:
1. massai, kenya and the inuit of canada populations consume food rich in meat/fat which have saturated and monounsaturated fat- yet CHD is almost unknown.

20
Q

B. Carbohydrates & Lipids

25.Evaluate how health claims about lipids are assessed

strengths and limitations

A

strengths:
- testing for correlation
- if the data is being compared
- how widely spread the data is (stdev error bars)
- has the difference been assessed statistically

limitations:
- measure of health validity? test?
- sample size needs to be large
- is the data generalizabile or selective
- human or animal trials? if animal, how applicable?
- were the controlled variables controlled?
- were the levels and frequency of lipids realistic?
- how rigorous and reliable were the methods to gather the data (ex. survey has bias)

21
Q

C. Proteins & Enzymes

27.Draw a molecular diagram to show the formation of a peptide bond.

type bond/reaction/the groups that make one of the products/where form

A

learn how to draw

type of bond= peptide bond
reaction= polymerisation (condensation of amino acids)

groups: carboxyl (OH) and amine group (NH2). the OH reacts with one of the Hs to form water as a product, along with the di- or poly-peptide

where formed: in the ribosomes polypeptides are synthesized

22
Q

C. Proteins & Enzymes

28.State that there are 20 different amino acids in polypeptides synthesized on ribosomes (encoded by dna) and that these amino acids can be modified after the polypeptide has been formed.

name an example and why it is done

A

hydroxproline is a modification of proline after the polypeptide is formed.
done to increase the stability of the collagen triple helix

23
Q

C. Proteins & Enzymes

30.Outline how 20 different amino acids enables virtually infinite polypeptide diversity.

three key ideas to the range of polypeptides and calculation

A
  1. any length
  2. 20 diff amino acid combinations
  3. amino acids in any order or combination

twenty to the power of amino acids will give you the number of possible polypeptide formations

24
Q

C. Proteins & Enzymes

31.Explain how amino acid sequence of polypeptides is coded for by genes.

aka central dogma of genetics

A

DNA codes for RNA in the nucleus through he process of transcription. mRNA codes for the sequence of amino acids on the polypeptide chain in the ribosomes (which is in the cytoplasm) via translation

25
Q

C. Proteins & Enzymes

32.Outline with examples how a protein may consist of a single polypeptide or more than one polypeptide linked together.

4 examples. list # of polypeptides, example, and what the protein does

A

a) Lysozyme
- 1 polypeptide
- the enzyme in secretions like mucus and tears
- kills the bacteria by digesting the peptidoglycan in the cell walls

b) Integrin
- 2 polypeptides
- membrane protein used to make connections between structures inside and outside the cell

c) Collagen
- 3 polypeptides
- structural protien in tendons, ligaments, skin, blood vessel limits
- provides high tensile strength w/limited stretching

d) hemoglobin
- 4 polypeptides
- transport protien in red blood cells
- binds oxygen in the lungs and releases it in the tissues with a reduced oxygen concentration

26
Q

C. Proteins & Enzymes

33.HL: Outline how amino acid sequence determines the three-dimensional conformation of a protein
SL: differentiate between globular and fibrous protiens

SL-Rgroup locat,shape,function,solubility,AA sequence,stability,examples

A

fibrous
location of r-group: exposed to H2O
shape: long and narrow
function: structural (strength/support)
solubility: insoluble
amino acid sequence: repetitive
stability: less sensitive to changes in heat, pH etc.
examples: collagen, myosin, fibrin, actin, keratin, elastin

globular
location of r-group: folded into the core of the molecule away from the water
shape: rounded and spherical
function: functional (catalytic, transport etc.)
solubility: soluble
amino acid sequence: irregular
stability: more sensitive to changes in heat, pH etc.
examples: catalyse, hemoglobin, insulin, immunoglobin

27
Q

C. Proteins & Enzymes

34.Explain denaturation

what is it, how is it done, and what can cause it

A

defn: the change to the conformation of a protein.
how: the 3D conformation of proteins is stabilized by bonds or interactions between R-groups of amino acids within the molecule. these bonds and interactions are relativley weake and can be broken.
causes: heat- vibrations can break intermolecular bonds. pH- changes the charges on the R-groups, breaking ionic bonds or causing new ionic bonds to be formed.

28
Q

C. Proteins & Enzymes

35.List a wide range of protien functions

12- function, description and examples

A
  1. function: catalysis, ex: rubisco
    - self explanatory

2.function: muscle contraction, ex: actin and myosin
- muscle contraction uses in locomotion and transport around the body

3.function: cytoskeletons, ex: tubulin
- tubulin is a subunit of microtubules that give animal cells their shape and pull apart chromosomes during mitosis

4.function: tensile strengthening, ex: collagen
- fiborus proteins give tensile strength needed for skin, tendons, ligaments, and blood vessel walls

5.function: blood clotting, ex: fibrin
- forms a network that raps red blood cells and platelets

6.function: transports nutrients and gases, ex: haemoglobin
- protien in blood help transport oxygen, co2, iron and lipids

7.function: cell adhesion, ex: integrin protiens
- adhesive adjacent animal cells

8.function: membrane transport, ex: sodium channel protein
- facilliatated diffusion, active transport and electron transport

9.function: hormones, ex: insulin
- both protein and hormone

10.function: receptors, ex: rhodopsin
- binding sites in membranes and cytoplasm for hormones, neurotransmitters, tastes, and smells, also receptors for light in the eye and in plants

11.function: packing of DNA, ex: histones
- associated with DNA and help chromosomes condense in mitosis

12.function: immunity, ex: immunoglobulins
-most diverse group of proteins, as cells can make a huge number of antibodies.

bold is easy to memorize if only need to know some

29
Q

C. Proteins & Enzymes

36.Outline the functions of rubisco, insulin, immunoglobin, rhodopsin, collagen, and spider silk.

A

Rubisco:
- enzyme
- catalyzes the reaction that fixes CO2 in the air
- ex. high concent in leaves and algal cells

insulin:
- hormone
- signals cells (ex. liver) to absorb glucose and help reduce the glucose concentration of the blood
- secreted by beta cells in the pancreas and transported by blood

immunoglobulins:
- antibodies: protective protiens in your immune system
- two antigens can bond to each ‘arm’ of the protein
- binding sites differ greatly thus responding to a wide array of pathogens

rhodopsin:
- pigment: absorbs light
- present in rod cells in the retina
- consists of opsin polypeptode surrounding a retinal prosthetic group
- retinal absorbs single photon of light -> changes shape ->change to the opsin -> rod cell send nerve impulse to the brain

collagen:
- rope like proteins made of three polypeptides wound together
- has many different forms
- ~quarter of human body is made of collagen
- forms mesh of fibres in skin, blood vessel walls etc. which prevents it from tearing and increses tensile strength.
- forms part of teeth and bones- helps prevents fractures and cracks

spider silk:
- different types and functions
- dragline silk is stronger than steel and tougher than kevlar (tough fibre)
- some regions seem like a disordered tangle, and when first made the polypeptide forms parallel arrays
- when stretched the polypeptide gradually extends, making the silk extendable, and high tensile strength

30
Q

C. Proteins & Enzymes

37.Explain what a proteome is

compare to genome

A

genome: all the genes of a cell, tissue or organism.
proteome: all the proteins of a cell, tissue or organism.

enviormental factors can affect what protein should be formed and how much of it needs to be made- this affects overall proteome

proteome> genome
- approx. 20,000 genes in your genome code for approx 10x as many proteins

31
Q

C. Proteins & Enzymes

38.Define the term enzyme

A

A globular protien that increases the rate of a biochemical reaction by acting as a catalyst. a catalyst lowers the activation energy threshold by binding the substrate to the active site, the bonds in the substrate are weakned, thus lowere Ea and are easily broken.

32
Q

C. Proteins & Enzymes

39.Explain enzyme structure and function including the concepts: active site, enzyme-substrate specificity, enzyme kinetics and enzyme catalysis.

A
  1. active site
    -function: after the enzyme and substrate bind on the active site it catalyzes the reaction
    -structure: the area on the enzyme where the substrate would bind
  2. enzyme-substrate specificity:
    -function: only substrates and enzymes that fit exactly react- very specific. induced fit does not explain this.
    -structure: seen in the lock and key model, where enzyme and substrate fit exactly
  3. enzyme kinetics
    - function: the act of collisions occuring between enzymes and substrates.
    - stucture: most enzyme reactions occur when substrates are dissolved in water because the molecules are able to move randomly- colliding with the enzyme. If not immobilized (ex. bound to a cell membrane) the enzyme can move too, however enzymes tend be larger than the substrate(s) and therefore move more slowly.
  4. enzyme catalysis
    - function: when enzymes and substrates collide successfully to result in catalysis of the reaction
    - structure: only successful with correct orientation (active site is aligned correctly) and with sufficent energy (when binding to overcome energy barrier).
33
Q

C. Proteins & Enzymes

40.Contrast the lock-and-key and induced fit models of enzyme function.

know how to draw it to because its good for understanding

A

Lock and Key:
- lock and key suggests only one enzyme would catalyze a reaction
- structurally: the 3D stucture of the active site is specific to the substrate- if they dont fit, it won’t react
- chemically: if the substrate is not chemically attracted to the active site so they won’t react. the polar regions of the amino acid (substrate) are attracted to the active site of the enzyme.

Induced fit:
- some enzymes can catalyze multiple reactions
- structurally: as a substrate approches an enzyme it induces comformational change in active site- changes shape to fit substrate. the activation energy decreases and enzyme reverts back to original shape.
- chemically: more enzymes are attracted to multiple reaction because of conformational change

34
Q

C. Proteins & Enzymes

41.Outline the factors that affect enzyme activity and accurately draw and label a graph that illustrates each.

list 3 factors and explain
obviously learn how to draw and label

A
  1. Temperature
    - low temp= insufficient thermal and kinetic energy for activation of enzyme-catalyst reaction, which is why at low reaction rate and temp the graph is low
    - as temp increases the speed and KE of both the enzyme and substrate increase resulting in more frequent successful collisions. this us why the reaction rate increases from low to high temp in the x-axis
    - HOWEVER, there is always an optimal temperature for every enzyme to which the rate of reaction would also be high.
    - After this optimal temp. the graph is shown to decrease rapidly. this is because at high temperatures the enzyme stability decreases. this is because molecular vibrations by the kinetic energy will cause the H-bonds holding the enzyme to break. this then causes the enzyme (mainly polar active site) to loose shape (conformation) and denature= loss in enzyme activity
    - ex. optimal temperature for enzymes in human cells are usually around human body temperature (37.5 oC).
  2. pH
    - changing the pH will alter the charge of the enzyme (R-group). this affects the protien solubility and possibily the shape of the molecule.
    - changing the shape will change the active site form, diminishing its ability to bind to the substrate- thus affecting enzyme function.
    - There is an optimal pH for each enzyme and moving outside of this range will diminish the rate of reaction. ex. pepsin has an optimal pH of 2
  3. Substrate concentration
    - increasing the substrate concentration will increase the rate of reaction
    - the optimum concentration of the substrate concentration will be when all active sites are full and working at max efficency.
    - any increase in concentration beyond the optimum will have no added effect as there will be no free active sites for reactions
35
Q

C. Proteins & Enzymes

42.Explain how denaturation affects enzyme action.

A

if an enzyme denatures, the active site will change it’s shape respectively, therefore the substrate will no longer be able to bind to it.

36
Q

C. Proteins & Enzymes

43.Outline enzyme immobilization and its advantages.

define/3 ways an enzyme can be immobilized/advantages to immobilization

A

enzyme immobilization: when an enzyme is attarched to a certain material so their movement is restricted

three ways enzymes can be immobilized:
1. aggregate enzymes by bonding them together
2. attached to surfaces ex. in cell membranes
3. entrapped in a gas ex. alginate gel beads

advantages:
1. concentration of the substrate can be increased easily as the enzyme is fixed. this will increase the rate of reaction
2. recycled enzymes can be used many times and immobilized enzymes are easy to seperate from the reaction mixture, resulting in cost saving
3. seperation of the products is straight forward/ also means reaction can be stopped at correct time
4. stability of the enzyme to changes in temp and pH is increased, thus reducing the rate of degradation- resulting in cost saving

37
Q

C. Proteins & Enzymes

44.Outline a method of producing lactose-free milk and its advantages.

5 (4) steps and 4 reasons why its done

A
  1. lactase is obtained most commonly from yeast (or bacteria)
  2. lactase is bound to the surface of alginate beads
  3. milk is passed (repeadetly) over the beads
  4. the lactose is broken doen into glucose and galactose
  5. the immobilized enzyme remains are to be used again and does not affect the quantity of the lactose free milk

advantages:
- for lactose intolerant people
- to increase the sweatness of milk negating the need for artifical sweetners
- to reduce the crystilization of ice creams (glucose and galactose are more soluble than lactose)
- shortneing the production of yougurts or cheese (bacteria ferment glucose and galactose more readily than lactose)

38
Q

C. Proteins & Enzymes

45.Design an experiment that quantitatively tests the effects of temperature, pH or substrate concentration on the activity of an enzyme.

A

Lab done in class on substrate concentration

39
Q

C. Proteins & Enzymes

29.Outline the hypothesises that attempts to explain why almost all organisms assemble polypeptides from the same amino acids.

A

Hypotheses:

  1. these 20 amino acids were the ones first produced by chemical processes on earth before the origin of life- so all organisms continued to use them. if there were more amino acids present then they would have been used
  2. they are the ideal 20 amino acids for making a wide range of proteins, so natural selection will always favour the organisms that use them.
  3. all life has evolved from a single ancestral species, which used these 20 amino acids. because of the way the polypeptides are made by ribosomes, it is difficult for any organism to change the repertoire of amino acids, either by removing existing ones or by adding new ones.
40
Q

C. Proteins & Enzymes

26.Explain how proteins are formed from amino acids.

A

A ribosome condenses two amino acids into a dipeptide forming a peptide bond. multiple amino acids would create a polypeptide chain also known as a protein

41
Q

A. Chemical Elements & Water

6.Draw molecular diagrams of glucose, ribose, a saturated fatty acid and a generalized amino acid.

learn how to draw

A

learn to draw

42
Q

A. Chemical Elements & Water

7.Identify biochemical as carbohydrate, lipid or protein from molecular diagrams.

mention 4 main carbs, and key factors for each to differentiate

A

CARBS:
1. Glucose
2. Galactose
3. Fructose
4. Ribose
1&2 hexose, 3&4 pentose
1 & 2 have the same pattern, but different dimension in space
learn how to draw glucose and ribose, learn how to identify fructose and galactose

LIPIDS:
Lipids are glycerol combined with 1, 2 or 3 fatty acids, therefore triglycerides are lipids
hydrocarbon tail with carboxyl group (carbonyl group C=O that has a hydroxyl group O-H attached to the carbon atom)
learn how to draw, and identify monounsaturated, polyunsaturated, and saturated

Protiens:
have an amine group (NH2) and carboxyl group at opposite ends with an R group oriented at the top, bottom, left or right.
learn how to identify

43
Q

A. Chemical Elements & Water

Define metabolism

A

Metabolism describes the totality of chemical processes that occur within a living organism in order to maintain life.

44
Q

A. Chemical Elements & Water

9.Contrast anabolism and catabolism

A

Anabolism
- metabolic reactions that build up complex molecules from simpler ones
- The synthesis of organic molecules via anabolism typically occurs via condensation reactions
- Condensation reactions occur when monomers are covalently joined and water is produced as a by-product

Catabolism
- metabolic reactions that break complex molecules down into simpler molecules
- The breakdown of organic molecules via catabolism typically occurs via hydrolysis reactions
- Hydrolysis reactions require the consumption of water molecules to break the bonds within the polymer

45
Q

A. Chemical Elements & Water

11.State that the existence of hydrogen bonds is theoretical but that we can assume that they exist if there is evidence, if it helps to predict behaviour, if it has not been falsified and if it helps to predict and explain natural phenomenon.

just something to remember- refresh: what is a h-bond

A

Hydrogen bonds are electrostatic attractions between a hydrogen atom and more electronegative elements like N, O, and F.
It’s FON to hydrogen bond!
strongest intermolecular force!