Biological Molecules Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

Why is water a polar molecule?

A

Because of the unequal distribution of electrons (polarity) despite being covalent. The electrons are pulled towards oxygen so it’s slightly negative while the hydrogens are slightly positive.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Why are water molecules cohesive?

A

The polarity (unequal distribution of electrons making the oxygen negative and hydrogen positive) means the molecules stick together with hydrogen bonds.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

How many hydrogen bonds can water make in solid, liquid and gas form? Why?

A

Ice - 4 bonds
Liquid- 2 or 3 because they’re always moving past each other and breaking and reforming due to the weak hydrogen bonds.
Gas- 0

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What’s adhesion and how does this as well as cohesion help in a xylem vessel?

A

The polar water molecules sticking to another material with polar properties (slightly positive or negative).
In a xylem, the vessel walls are polar so water molecules are attracted to it. This and the attraction of the water molecules to each other (cohesion) helps to transport water up the leaves in a capillary action.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Why is water a polar solvent?

A

It will dissolve things that are polar (glucose) and ionic (salt).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Why will water dissolve things that are ionic as well as polar?

A

The positive end of the water molecule (hydrogen) will be attracted to the negative ion and the negative end of the water molecule (oxygen) will be attracted to the positive ion.

This means ions will be totally surrounded by water molecules and they’ll dissolve.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Why is water used as a transport medium? Give examples

A

Because it’s a solvent and metabolite (involved in many metabolic reactions).
Plants- xylem, phloem
Animals- plasma in the blood

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Why does water provide a stable environment for organisms to live in.

A

Because it’s thermostable: buffers/resists change in temp

It has a high specific heat capacity so needs lots of energy to raise the temperature of 1kg by 1 degree.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Why does water have a high latent heat of vaporisation from liquid to gas?
Why does hand sanitiser make your hands cold?

A

Because a lot of energy is needed to break the hydrogen bonds between water molecules and change the state.

Molecules with enough energy evaporate, carrying heat away (evaporation causes cooling).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What allows aquatic plants and algae to photosynthesise?

A

The transparency of water.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Why does ice float?

A

As water freezes it expands (molecules held further apart by hydrogen bonds) so frozen water is less dense than liquid (which has less hydrogen bonds) and therefore floats.

The frozen ice layer insulates the water below so the water below doesn’t freeze (allowing some organisms to survive).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Give 6 examples of inorganic ions biological significance in organisms.

A

IRON IONS- found in haemoglobin where they play a role in the transport of oxygen and are used in ferrodoxin in photosynthesis and is an electron carrier in some bacteria.
PHOSPHATE IONS- play a structural role in DNA molecules as the sugar-phosphate backbone of DNA structure.
Bonds between phosphate ions store energy in ATP molecules.
Phospholipids make up the plasma membrane.
HYDROGEN IONS- important in determining the PH of solutions and therefore the functioning of enzymes.
SODIUM IONS- important in the transport of glucose + amino acids across plasma membranes and they generate resting and action potentials in neurons.
NITROGEN- used in chlorophyll.
CALCIUM- an extracellular component of bone matrix.
It forms an exoskeleton.
It stimulates synaptic transmission between neurons and is used in muscle contraction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What does water dissolve as a solvent?

A

Gases (oxygen, carbon dioxide)
Wastes (ammonia + urea)
Inorganic ions + small hydrophilic molecules (amino acids, monosaccharides + ATP)
Enzymes who’s reactions take place in solution.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Water in metabolism

A

Used to break down complex molecules by hydrolysis (proteins to amino acids).
Produced in condensation reactions.
Chemical reactions take place in aqueous solutions.
It’s a Major raw material in photosynthesis.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What do organic compounds have and why are they non-polar?

A

Organic compounds have C-H bonds.

They’re non-polar because the electrons are evenly distributed.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Why are a large number of types and sizes of molecule all based on carbon?

A

Carbon atoms very readily form bonds with other carbon atoms which allows a sequence of carbon atoms of various lengths to be built up. These form a backbone along which other atoms can be attached.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

How do monomers and polymers link and give examples of both.

A

Monomers are individual molecules which join in long chains called polymers.

Carbohydrates-The monomers monosaccharides join in chains to make polysaccharides.
The monomers amino acids join in chains to make proteins.
The monomers nucleotides join to make the polymers nucleic acids (DNA and RNA).
Glycerol and fatty acids join to make triglycerides (fat).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What four elements are most polymers made up of?

A

Carbon, hydrogen, oxygen and nitrogen.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Monosaccharides definition and examples

A

E.g. glucose, galactose and fructose.

Monosaccharides (simple sugars) are sweet, soluble substances (organic molecules) that act as building blocks for more complex carbs (polysaccharides).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What’s a disaccharide and how is it made?

A

A disaccharide is the combination of two monosaccharides.
A disaccharide is formed through a condensation reaction: when the monosaccharides join, a molecule of water is removed and the bond formed is called a glycosidic bond.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What’s the opposite of a condensation reaction?

A

A hydrolysis reaction.

When water is added to a disaccharide (or polysaccharide) it breaks the glycosidic bond releasing the monosaccharides.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

What’s the general formula for a monosaccharide?

A

(CH2O)n

n= number of carbon atoms (3-7)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Glucose

A

A monosaccharide.
Glucose is a hexose (6 carbons sugar) with the formula C6H12O6.
Glucose has two isomers (same chemical formula but different arrangement of atoms): alpha glucose and beta glucose.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

What’s a reducing sugar?

A

Reducing sugars are sugars that can donate electrons (or reduce) another chemical (in the case of the practical: Benedict’s reagent) (OILRIG).

All monosaccharides and some disaccharides (except sucrose) are reducing sugars.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

What happens to the Benedict’s reagent when it’s heated in a water bath with a reducing sugar?

A

Benedict’s reagent is an alkaline solution of copper (II) sulphate. When a reducing sugar is heated with the Benedict’s reagent it forms an insoluble red precipitate of copper (I) oxide.
Electrons are donated from the reducing sugar to the Benedict’s reagent.
Cu2+ + e- = Cu+

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

How to make the non-reducing sugar sucrose (disaccharide) int two monosaccharides to make it a reducing sugar.

A

If the Benedict’s reagent stayed blue it’s a non-reducing sugar.

  • To make sucrose a reducing sugar you perform hydrolysis by adding hydrochloric acid and heating in a water bath for 5 mins. This should separate the disaccharide into two monosaccharides making two reducing sugars.
  • Then add neutraliser (sodium hydrogen carbonate) until it stops fizzing and is alkaline (or use litmus paper).
  • Retest the resulting solution by heating with 2cm3 of Benedict’s reagent in a water bath for 5 mins.

If a non-reducing sugar as present in the original sample the Benedict’s will turn orange-brown. This is due to the reducing sugars that were produced from the hydrolysis of the non-reducing sugar.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Disaccharide examples

A

Glucose + glucose = maltose
Glucose + fructose = sucrose
Glucose + galactose = lactose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

What are polysaccharides?
Soluble or insoluble? Why?
What happens when they’re hydrolysed?
Give 2 examples.

A
  • Polysaccharides are polymers formed by combining together many monosaccharides that are joined by glycosidic bonds through a condensation reaction.
  • Polysaccharides are insoluble as they’re very large molecules which make them suitable for storage.
  • When hydrolysed they break down into disaccharides or monosaccharides.
  • Starch is found in many parts of plants (in form of granules or grains) e.g. chloroplast. It’s formed by the joining of 200-100,000 alpha glucose molecules by glycosidic bonds in a series of condensation reactions.
  • Cellulose gives structural support to plant cells.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Test for starch.

A

Starch is easily detectable as it changes the colour of iodine in potassium iodide from yellow to blue/black.

  • Put 2cm3 of the sample in a test tube or 2 drops into spotting tiles.
  • Add 2 drops of iodine solution + shake or stir.
  • Presence of starch = blue/black.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

How is starch suited to its role in energy storage?

A
  • Insoluble, doesn’t effect water potential, so water isn’t drawn into the cells by osmosis.
  • large and insoluble, doesn’t diffuse out of cells.
  • compact, so a lot of it can be stored in a small space.
  • When hydrolysed it forms alpha glucose which is both easily transported and readily used in respiration.
  • the branched form has many ends, each of which can be acted on by enzymes simultaneously meaning glucose monomers are released very rapidly.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

What two polysaccharides is starch made up of?

A

Amylose and amylopectin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

Amylose

A

This and amylopectin make up starch

  • Formed by alpha glucose monomers.
  • alpha 1,4 glycosidic bonds between the monomers.
  • The chain forms a coiled shape.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

Amylopectin

A

This and amylose make up starch.

  • Formed from alpha glucose monomers.
  • alpha 1,4 and alpha 1,6 glycosidic bonding between the monomers.
  • Branch shape due to the extra alpha 1,6 glycosidic bonding.
  • More branches: more easily hydrolysed (because there’s more places where the enzyme can work) to glucose or maltose to provide energy when needed.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q
Glycogen.
Where found?
Structure
Main role
How stored and where found in body?
A
  • Found in animal, fungi and bacterial cells.
  • Very similar structure to amylopectin.
  • formed from chains of monosaccharide alpha glucose but there’s less alpha 1-4 glycosidic bonds and more alpha 1,6 glycosidic bonds (because it’s highly branched so produces lots of glucose).
  • Main role: energy storage.
  • Also in small granules (like starch), found mainly in the muscles and liver.
  • Animals need more glucose than plants because they’re more active so they have more branches in glycogen than in starch.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

Starch and glycogen similarities.

A

-Joining of alpha glucose.
Compact- so a lot can be stored in little space, due to their structure (coiled like a slinky).
-Provide easy access to glucose (energy source)- glucose released by hydrolysis of glucose molecules from multiple ends (branches).
-Large and insoluble so it doesn’t diffuse out of cells or affect the water potential.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

How is the structure of cellulose suited to its function of providing support and rigidity?
How does the cellulose cell wall prevent the cell from bursting as water enters it by osmosis?

A
  • Cellulose molecules are made up of beta glucose and so form long straight, unbranched chains.
  • These cellulose molecular chains run parallel to each other and are crossed linked by weak hydrogen bonds which add collective strength.
  • These molecules are grouped to form microfibrils which in turn are grouped to form fibres all of which provide more strength.

-By exerting an inward pressure that stops any further influx of water. As a result, living plant cells are turgid and push against one another, making non-woody parts of the plant semi-rigid. This is important in maintaining stems and leaves in a turgid state so they can provide the maximum surface area for photosynthesis.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

Lipids characteristics

A
  • They contain carbon, hydrogen and oxygen.
  • The proportion of oxygen to carbon and hydrogen is smaller than in carbohydrates.
  • non-polar due to large % of Cs and Hs and so are Insoluble in water (hydrophobic).
  • Soluble in organic solvents such as alcohols and acetone.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

Roles of lipids

A
  • Phospholipids contribute to the flexibility of membranes and the transfer of lipid-soluble substances across them.
  • source of energy (when oxidised, lipids provide more than twice the energy as the same mass of carbohydrates + release valuable water.
  • Waterproofing (they’re insoluble in water + therefore good for waterproofing. Plants and insects have waxy lipid cuticles that conserve water while mammals produce an oily secretion from the sebaceous glands in the skin).
  • Insulation (fats are slow conductors of heat + when stored beneath body surface help to retain body heat. Also act as electrical insulators in the myelin sheath).
  • protection (fat is often stored around delicate organs such as the kidney).
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

Properties of saturated fatty acids.

A

E.g. meats, butter, dairy.
- Contain only C-C bonds (no double bonds between carbon atoms because all the carbon atoms are linked to the maximum possible number of hydrogen atoms) so form linear hydrocarbon chains.
- Fatty acids can pack closely together.
Strong attraction between fatty acid chains.
-High melting points
-Solid at room temp.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

Properties of unsaturated fatty acids.

A

E.g. vegetable oils

  • Contain one or more C=C double bond (causing hydrocarbon chains to bend).
  • Non-linear chains don’t allow fatty acid molecules to pack closely together.
  • Fewer interactions between fatty acid chains, so weaker attractions.
  • Low melting points
  • liquid at room temp
41
Q

Triglycerides

A

Three fatty acids combined with glycerol (glyceride). Each fatty acid forms an Ester bond with glycerol in a condensation reaction. Hydrolysis of a triglyceride produces glycerol and 3 fatty acids.

The glycerol molecule is the same so the variations in properties of different fats and oils comes from variations in the fatty acids.
All 70 fatty acids have a carboxyl (—COOH) group with a hydrocarbon chain attached.

Saturated- chain has no C-C double bonds because all carbon atoms are saturated with hydrogen.
Mono-unsaturated- single double bond.
Polyunsaturated- more than one double bond.
More double bonds, the lower the melting point.

42
Q

How does the structure of triglyceride relate to its properties.

A
  • have a high ratio of energy- storing carbon- hydrogen bonds to carbon atoms and are therefore an excellent source of energy.
  • Low mass to energy ratio, making them good storage molecules because much energy can be stored in a small volume. This is especially beneficial to animals as it reduces the mass they have to carry as they move around.
  • Being large, non-polar molecules, triglycerides are insoluble in water. As a result their storage does not affect osmosis in cells or the water potential of them.
  • As they have high ratio of hydrogen to oxygen atoms, triglycerides release water when oxidised and therefore provide an important source of water, especially for organisms living in dry dessert.o
43
Q

What are the two parts phospholipids are made up of and why.

A

Phospholipids are similar to lipids except that one of the fatty acid molecules is replaced by a phosphate molecule.
Fatty acid molecules repel water (are hydrophobic) while phosphate molecules attracts water (are hydrophilic). A phospholipid is therefore made up of two parts:

A hydrophilic head: which interacts with water (attracted to it) but not with fat.
A hydrophobic tail: which orients itself away from water but mixes readily with fat.

44
Q

Why are phospholipids polar?

A

Because it’s a molecule that has two ends (poles) that behave differently: when they’re placed in water they position themselves so the hydrophilic head heads are as close to the water as possible and the hydrophobic tails are as far away from the water as possible.

45
Q

How is the structure of phospholipids related to their properties?

A
  • They’re polar molecules, having hydrophilic phosphate head and a hydrophobic tail of two fatty acids. This means in an aqueous environment, phospholipid molecules form a bilayer within cell surface membranes. As a result a hydrophobic barrier is formed between the inside and outside of a cell.
  • The hydrophilic phosphate heads of phospholipid molecules help to hold at the surface of the cell surface membrane.
  • The phospholipid structure allows them to form glycolipids by combining with carbohydrates within the cell surface membrane. These glycolipids are important in cell recognition.
46
Q

Test for lipids

Why?

A

Emulsion test:

  • Take a completely dry and grease free test tube.
  • Add 5cm3 of ethanol to 2cm3 of the sample being tested.
  • Shake tube thoroughly to dissolve any lipid in the sample.
  • Add 5cm3 of water and shake gently.
  • Milky white emulsion indicates presence of a lipid.
  • As a control, repeat the procedures using water instead of the sample, the final solution should remain clear.

-The cloudy colour is due to lipid in the sample being finely dispersed in the water to form an emulsion. Light passing through this emulsion is refracted as it passes from oil droplets to water droplets, making it appear cloudy.

47
Q

What’s the polymer that’s made up of amino acid monomers called?
What can these polymers be combined to make?

A

Polypeptide (chain).

Polypeptides combine to make proteins.

48
Q

Structure of an amino acid.

A

Every amino acid has a central carbon atom to which four different chemical groups are attached:

  • amino group (—NH2)- a basic group from which the amino part of the name amino acid is derived.
  • carboxyl group (—COOH) - an acidic group which gives the amino acid the acid part of its name.
  • hydrogen atom (—H)
  • R (side) group- a variety of different chemical groups. Each amino acid has a different R group. These 20 naturally occurring amino acids differ only in their R (side) group.
49
Q

The formation of a peptide bond of a dipeptide.

How can they be broken?

A

Amino acid monomers combine to form a dipeptide in a condensation reaction. The water is made by combining an —OH from the carboxyl group of one amino acid with an —H from the amino group of another amino acid. The amino acids then become linked by a new peptide bond between the carbon atom of one amino acid and the nitrogen atom of the other.
They can be broken by hydrolysis (addition of water) to give two amino acids.

50
Q

Primary structure of proteins

A

Hundreds of amino acid monomers joined together through polymerisation is called a polypeptide chain (primary structure).
The sequence of amino acids in a polypeptide chain forms the primary structure of any protein. (This sequence is determined by DNA).

It’s the primary structure of a protein that determines its shape and therefore function so a change in a single amino acid in this primary sequence can lead to a change in the shape of the protein and therefore stop it carrying out its function. (Protein shape is specific to function).

Normally, a protein is made up of a number of polypeptide chains though a simple protein can just consist of one.

Formed between C-N
Unbranched

51
Q

Secondary structure of proteins

A

The linked amino acids that make up polypeptide possess —NH and —C=O groups on either side of every peptide bond.
The hydrogen of —NH has an overall positive charge while the oxygen of —C=O has an overall negative charge.
These two groups therefore readily form weak hydrogen bonds which causes the long polypeptide chain to be twisted into a 3D shape e.g. the coil alpha helix.
Beta sheet is also stabilised by hydrogen bonds.

52
Q

Tertiary structure

A

The alpha helixes of the secondary protein structure twisted and folded to make the complex, 3D structure of each protein: tertiary structure. The 3D shape of a protein is important in how it functions and how it’s recognised by other molecules and therefore the specific way it interacts with them.
Joined by dipeptide, ionic, hydrogen bonds and hydrophobic interactions between the R groups. Positive R groups attract negative R groups.
The structure is maintained by these bonds:

Disulfide bridges: fairly strong + not easily broken.

Ionic bonds: formed between any carboxyl and amino groups that aren’t involved in forming peptide bonds. Weaker than disulfide bonds and easily broken by changes in PH.

Hydrogen bonds: numerous but easily broken.

Hydrophobic interactions

53
Q

Quaternary structure of proteins

A

Large proteins often form complex molecules containing a number of individual polypeptide chains that are linked in various ways (Held together by the same 4 R group bonds as tertiary).
There may also be non-protein groups associated with the protein, called prosthetic groups.
E.g. haemoglobin.
Haemo-prosthetic (non-protein) group.
Globin-globular protein.

54
Q

Test for proteins

A

The Biuret test detects peptide bonds:

  • Place a sample of the solution to be tested in a test tube and add an equal volume of sodium hydroxide solution at room temp.
  • Add a few drops of very dilute (0.05%) copper (II) sulfate solution and mix gently.
  • A purple coloration indicates the presence of peptide bonds and hence a protein. If no protein is present, the solution remains blue.
55
Q

Globular proteins

A
  • Spherical shape.
  • soluble in water because they have hydrophilic amino acids on their surface so hydrophilic R groups can interact with water mulecules while the hydrophobic amino acids are in the centre of the protein.
  • E.g. enzymes, (lysozyme) haemoglobin and insulin.
  • Carry out metabolic functions.
56
Q

Fibrous proteins

A

E.g. collagen (strengthens bones, cartilage, tendons, ligaments and skin), gluten
They have structural functions.

57
Q

Molecular structure of collagen

A
  • primary structure is an unbranched polypeptide chain.
  • in the secondary structure the polypeptide chain is very tightly wound .
  • lots of amino acid, glycine helps close packing.
  • in tertiary structure the chain is twisted into a second helix.
  • its quaternary structure is made up of 3 polypeptide chains wound together in the same way as individual fibres are wound together in a rope.
  • the individual collagen polypeptide chains in the fibres are held together by bonds between amino acids of adjacent chains.
  • the points where one collagen molecule ends and the next begins are spread throughout the fibre rather than all being in the same position along it.
58
Q

Induced fit model of enzyme action

A

This proposes that the active site forms as the enzyme and substrate interact (complimentary active site and substrate.)
The enzyme is flexible and can mould itself around the substrate in the way that a glove moulds itself to a hand. The enzyme has a certain general shape but this alters in the presence of a substrate. Once the product(s) has been made, the enzyme molecule resumes its original shape.

As it changes its shape, the enzyme puts a strain on the substrate molecule. This strain distorts a particular bond(s) in the substrate and therefore lowers the activation energy needed to break the bond.

59
Q

What’s an enzyme (what’s a catalyst).

A

Globular proteins that act as biological catalysts (have specific 3D shapes as a result of their sequence of amino acids).

Catalysts alter the rate of chemical reactions without undergoing permanent changes themselves; they can be reused repeatedly and are therefore effective in small amounts.

60
Q

For reactions like (sucrose + water= glucose + fructose) this to take place, what conditions must be satisfied?

A
  • the sucrose and water molecule must collide with sufficient energy to alter the arrangement of their atoms to form glucose and fructose (in a hydrolysis reaction).
  • the free energy of the products (glucose and fructose) ,must be less than that of the substrates (sucrose and water).
  • many reactions require an activation energy (minimum amount of energy needed to activate the reaction).
61
Q

What do enzymes as catalysts do?

A

Enzymes as catalysts lower the activation energy (make the hill or barrier lower) which must be initially overcome before the reaction can proceed. By the enzymes lowering the activation energy level, the enzymes allow reactions to take place at a lower temperature than normal. This enables some metabolic processes to occur rapidly at the human body temperature of 37 degrees (low in terms of chemical reactions). Without enzymes, these reactions would happen too slowly to sustain life as we know it.

62
Q

Enzyme structure

A

Globular proteins that have a specific 3D shape as a result of their sequence of amino acids (amino acids joined with hydrogen bonds).
The active site is made up of a relatively small number of amino acids and forms a small depression within the much larger enzyme molecule.
The molecule that the enzyme acts on is called the substrate. This fits neatly into into the complimentary active site to form an enzyme-substrate complex. The substrate molecule is held in the active site by bonds that temporarily form between certain amino acids of the active site and groups on th substrate molecule.

63
Q

A weakness of the lock and key model.

A

In this model, the enzyme is suggested to be (like a lock) a rigid structure. However scientists observed that other molecules could bind to enzymes at sites other than the active site, altering the activity of the enzyme. This suggested that the enzymes shape was being altered by the binding molecule.
It’s structure was therefore not rigid like this model suggests, but flexible (induced fit model).

64
Q

How does denaturation through PH happen (in detail)?

A

Changes in PH changes the charges on the R groups in the active site and affects the binding of the substrate to the active site.

Changes in PH changes the charges on the R groups in the protein and affects the hydrogen bonding and ionic bonds that stabilise the tertiary structure, leading to denaturation.

65
Q

Buffer solutions (salt and acid).

A

Resist changes in PH. Keep the PH of solution stable.

66
Q

Description and explanation of how enzyme concentration affects rate of reaction. (Graph)

A

As the enzyme concentration increases, the rate of reaction increases.

A high enzyme concentration increases the frequency of successful collisions.
This leads to an increase in enzyme substrate complexes being formed.
As a result there’s an increase in the rate of reaction.

67
Q

Description and explanation of how substrate concentration affects rate of reaction. (Graph)

A

It increases rapidly at first, but plateaus at the point of saturation where the increasing substrate concentration no longer affects rate of reaction.

As substrate concentration increases the frequency of successful collisions also increases. This leads to an increase in the number of enzyme substrate complexes being formed. As a result there’s an increase in the rate of reaction.
However when the substrate concentration becomes very high the enzyme becomes saturated with substrate. This means a further increase in substrate will not result in any more enzyme substrate complexes being formed.
So the reaction proceeds at a maximum rate that can’t be increased unless more enzyme is added.

68
Q

Enzyme inhibition (inhibitors).

A

Inhibitors are substances that directly or indirectly interfere with the functioning of the active site of a specific enzyme and so decrease the rate of reaction.

69
Q

Competitive inhibitors.

A

-Have similar shape to the substrate which allows them to bind and occupy the active site.
-Compete with substrate for active site.
-Binding isn’t permanent so when it leaves the active site another molecule can enter (substrate or inhibitor).
E.g. succinate and malonate in the Krebs cycle.

The graph for substrate concentration to rate of reaction is less steep when an inhibitor is present because the rate of reaction is reduced as the active sites are occupied with inhibitor not allowing enzyme substrate complexes to form.

Maximum rate can be achieved if the substrate levels are high enough.

70
Q

Non-competitive inhibitors.

A

-Attach to enzyme at the allosteric site.
-Binding causes a change in the tertiary structure of the enzyme therefore also changing the shape of the active site.
-This means the active site is no longer complimentary to the substrate so the substrate can no longer bind (so enzyme can’t catalyse the reaction).
E.g. cyanide

The graph stays flat because the active site is altered so the maximum rate can’t be achieved by raising the substrate levels.

71
Q

Feedback inhibition and negative pathways.

Metabolic pathways.

A

Allosteric enzymes can be used to control metabolic pathways using negative feedback.
The end product binds to the first enzyme in the pathway and inhibit it if too much product is formed (supply and demand).

Metabolic pathways are a sequence of chemical reactions where there are multiple steps and each step is catalysed by a different enzyme.
Hundreds of metabolic pathways occur in every cell.

72
Q

What 3 components are nucleotides made up of and what do they form when joined together?

A

Pentose sugar (has 5 carbon atoms).(pentagon).
A phosphate group (circle)
A nitrogen containing organic base: cytosine, thymine, uracil, guanine.

These are joined by condensation reactions to form mononucleotides.

73
Q

What bond is formed when two mononucleotides are joined in a condensation reaction?

A

Two mononucleotides (sugar, phosphate + base) can be joined in a condensation reaction between the deoxyribose sugar of one mononucleotide and the phosphate group of another. The bond formed is called a phosphodiester bond.

74
Q

What’s it called when two mononucleotides are joined?

A

Dinucleotide.

75
Q

What’s the continued linking of mononucleotides called?

A

Polynucleotide.

76
Q
Ribonucleic acid (RNA) structure.
Example of RNA function.
Types of RNA
A

Single, relatively short polynucleotide chain in which the pentose sugar is always ribose and the organic bases are adenine, guanine, cytosine and uracil.
One type of RNA transfers genetic info from DNA to the ribosomes (ribosomes are made from proteins and another type of RNA).
Another type of RNA is involved in protein synthesis

Messenger RNA
Ribosomal RNA
Transfer RNA.

77
Q

DNA structure.

A

Pentose sugar- deoxyribose.
Organic bases- adenine, thymine, guanine and cytosine.
DNA is made up of two long strands of nucleotides (polynucleotides) joined by hydrogen bonds between certain bases.

78
Q

DNA base pairings.

A

The bases are attached with hydrogen bonds.
Adenine - thymine
Guanine - cytosine
These bases are complimentary to each other.
The quantities of adenine and thymine in DNA are always the same and so are the quantities of guanine and cytosine.
Though the ratio of a and d to g and c varies from species to species.

79
Q

DNA double helix.

A

Polynucleotide chains are twisted around each other in a ladder like arrangement. I’m this way the uprights of phosphate and deoxyribose wind around eachother to form a double helix. They form the structural backbone of the DNA molecule.

80
Q

What makes DNA a stable molecule?

A
  • The phosphodiester backbone protects the more chemically reactive bases inside the double helix.
  • Hydrogen bonds link the organic base pairs forming bridges (rungs) between the phosphodiester uprights.
  • There are 3 hydrogen bonds between C and G so the higher the proportion of C-G pairings, the more stable the DNA molecule.
  • There are other interactive forces between the base pairings that hold the molecule together.
81
Q

Function of DNA

A

The hereditary material that passes genetic material through generations. There are around 3.2 million million base pairs of DNA in a mammalian cell meaning there’s almost an infinite variety of sequences of bases, providing genetic diversity within living organisms.

82
Q

Adaptations of DNA.

What makes it stable?

A
  • The very stable structure passes from generation to generation without significant change, so most mutations are repaired and persistent mutations are rare.
  • Its two separate strands are only joined with hydrogen bonds which allows them to separate during DNA replication and protein synthesis (zip).
  • many hydrogen bonds joining the separate strands are strong together.
  • It’s an extremely large molecule and therefore carries an immense amount of genetic information.
  • By having the base pairs within the helical cylinder of the deoxyribose-phosphate backbone, genetic information is to some extent protected from being corrupted by outside chemical and physical forces.
  • Base pairing leads to DNA being able to replicate and to transfer information as mRNA.
  • The function of DNA depends on the sequence of base pairings that it possesses. This sequence is important to everything it does and to life itself.
  • Hydrophobic bases are protected on the inside of the hydrophilic backbone.
83
Q

What is the explanation for the mice being injected with a dead harmful form and living safe form of pneumonia getting pneumonia?
Investigation into the reason.

A

The DNA provided the bacteria with the genetic information needed to make the virus and can be passed from one bacterium to another.

  • the living harmful bacteria found in pneumonia mice were collected and various substances were isolated from these bacteria and purified.
  • each substance was added to suspensions of living safe bacteria to see whether it would transform them into the harmful form.
  • the only substance that produced this transformation was purified DNA and when an enzyme that breaks down DNA was added, the ability to carry out the transformation ceased.
84
Q

3’ (3 prime) and 5’ (5 prime) carbon atoms.

A

The 5’ carbon has an attached phosphate group.
The 3’ carbon has an attached hydroxyl group.

When nucleotides are organised into the double strands of a DNA molecule, one strand runs in the 5’ to 3’ direction while the other runs in the 3’ to 5’direction. The two strands are therefore antiparallel.

Nucleic acids can only be synthesised ‘in vivo’ in the 5’ to 3’ direction.
This is because the enzyme DNA polymerase that assembles nucleotides into a DNA molecule can only attach nucleotides to the hydroxyl (OH) group on the 3’ carbon molecule.

85
Q

Base pairings

How many bonds between each?

A

Cytosine (3 H bonds) Guanine

Adenine (2 H bonds) Thymine

86
Q

What people used to think DNA was made out of VS what it’s actually made out of.

A

Proteins
Carbon, hydrogen, oxygen, nitrogen, sulphur.
Nucleic acids
Carbon, hydrogen, oxygen, nitrogen, phosphorus.

87
Q

What monomers and polymers is DNA made from?

What’s the enzyme that hydrolyses _____ into blank.

A

Monomers: nucleotides
Polymers: nucleic acids
Nucleic acids are information carrying polymers and are constructed by the condensation of nucleotide monomers.
The enzyme that hydrolyses nucleic acids into nucleotides is nucleases

88
Q

Pyrimidines and purines.

How deoxyribose more stable than ribose?

A

Pyrimidines:
Cytosine, thymine, uracil.
Single carbon-nitrogen ring with two nitrogen atoms

Purines:
Adenine, guanine.
Double carbon-nitrogen ring with four nitrogen atoms

Deoxyribose is ribose minus an oxygen atom, this makes it more stable and helps DNA maintain its integrity.

89
Q

Semi-conservative DNA replication.

A
  • The enzyme DNA helicase causes the DNA double helix to unwind and separate into two strands by breaking the hydrogen bonds between complimentary base pairs.
  • Each exposed strand then acts as a template for DNA replication to occur. Activated free nucleotides (nucleoplasm) are attracted to and hydrogen bond specifically to their complimentary bases on the exposed template strands by complimentary base pairing.
  • Once the newly added nucleotides have lined up they are then joined together by the enzyme DNA polymerase in the 5’ to 3’ direction, which catalyses the formation of phosphodiester bonds, forming a newly synthesised polynucleotide chain.
  • This results in two identical DNA molecules being produced, each of which contains one of the original DNA strands and one newly synthesised DNA strand. Semi-conservative replication.
90
Q

First generation: conservative, semi-conservative and dispersive and second generation dispersive.

A

Conservative: 2 lines found not valid
Semi-conservative: one intermediate line
Dispersive: one intermediate line.

Second generation
Dispersive: one intermediate line found not valid.

91
Q

Positioning of 14N and 15N lines at the first at the second generation semi- conservative replication.

A

First generation
Light 14N and dense 15N merge together in one intermediate line.

Second generation
Light 14N: top line
Dense 15N: bottom line

92
Q

What are the isotopes of nitrogen.

A

N15- dense original DNA

N14- light new DNA

93
Q

Structure of ATP

A

3 phosphates
Ribose sugar- sugar molecule with 5 carbon ring structure (pentose sugar) which acts as a backbone that the other parts are attached to.
Adenine- nitrogen containing organic base.

94
Q

How ATP stores energy.
Enzyme that catalyses the reaction ATP to ADP.
Equation.

A

The bonds between the phosphate groups are unstable, so they have a low activation energy and are easily broken. When they do break, they release a considerable amount of energy. The third phosphate is removed.

ATP + H2O = ADP + Pi + E
Adenosine triphosphate + water = adenosine diphosphate + inorganic phosphate + energy.
ATP is converted to ADP as water is added in a hydrolysis reaction.
The reaction is catalysed by the enzyme ATP hydrolase.

95
Q

Synthesis of ATP.

Enzyme that catalyses reaction ADP to ATP.

A

The conversion of ATP to ADP is a reversible reaction and therefore energy can be used to add an inorganic phosphate to ADP to make ATP.
The enzyme that catalyses this reaction is ATP synthase.
ADP is converted back to ATP as water is removed in a condensation reaction.

96
Q

What are the three ways that the synthesis of ATP from ADP occurs (addition of phosphate molecule to ADP.

A
  • In chlorophyll-containing plant cells during photosynthesis (photophosphorylation).
  • In plant and animal cells during respiration (oxidative phosphorylation).
  • In plant and animal cells when phosphate groups are transferred from donor molecules to ADP (substrate-level phosphorylation).
97
Q

What makes ATP a good energy donor but a bad long term energy store?

A

The instability of ATP’s phosphate bonds makes it a good energy donor but a bad long-term energy store (fats and carbs serve this purpose better). It’s an immediate energy source of a cell so cells don’t store large large quantities but maintain a few seconds supply that can be rapidly re-formed from ADP and Pi.

98
Q

Why is ATP a better immediate energy source than glucose?

A
  • ATP molecules release less energy for reactions than glucose molecules in smaller, more manageable quantities rather than the bigger, less manageable quantities.
  • The hydrolysis of ATP to ADP is a single reaction that releases immediate energy. The breakdown of glucose is a long series of reactions so the energy release takes longer.
99
Q

What energy requiring processes in cells is ATP used for?

Where is ATP made and why?

A

ATP can’t be stored so is continuously made within the mitochondria of cells that need it.

  • metabolic processes: ATP provides the energy needed to build up macromolecules from their basic units e.g. starch from glucose.
  • movement: ATP provides the energy for the filaments of muscle to slide past one another in muscle contractions and therefore shorten the overall length of a muscle fibre.
  • active transport: ATP provides the energy needed to change the shape of carrier proteins in plasma membranes. This allows molecules or ions to be moved against a concentration gradient.
  • secretion: ATP is needed to form the lysosomes necessary for the secretion of cell products.
  • activation of molecules: The inorganic phosphate released during the hydrolysis of ATP can be used to phosphorylate other compounds in order to make them more reactive, thus lowering the activation energy in enzyme-catalysed reactions. E.g. the addition of phosphate to glucose molecules at the start of glycolysis.