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Biology Revision Year 1 > Chapter 1 - Biological Molecules > Flashcards

Chapter 1 - Biological Molecules Flashcards

1
Q

describe a hydrogen bond

A

a hydrogen bond happens when the atom becomes polarised, this means that the negative part of one is attracted to the positive part of another.
hydrogen bonds are a weak electrostatic attraction

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2
Q

describe a van der wall bond

A

a van der wall bond forms as the charge of an atom changes with its orbit, creating an electrostatic attraction

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3
Q

what is a polymer?

A

a chain of monomers

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4
Q

how many types of amino acids are there?

A

20

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5
Q

<p>what are the different DNA bases? </p>

A

adenine, thymine, guanine, cytosine

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6
Q

what base replaces thymine in RNA?

A

uracil

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7
Q

<p>what is cellulose?</p>

A

<p>a polysaccharide made up of beta glucose. It makes up 40 - 60% of the cell wall in plants. It is structurally very strong because of intramolecular hydrogen bonds forming microfibrils. every other B glucose is inverted.</p>

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8
Q

what is starch made up of?

A

amylose - long unbranched

amylopectin - branched with 1,6 glycosydic bonds

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9
Q

what is glycogen?

A

a storage molecule in animals

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10
Q

what is Benedict’s test?

A

it works to find reducing sugars as the bond breaks in ketone or aldehyde (see diagram in notes) giving the solution it’s colour. Colour changes from blue to brick red.

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11
Q

how can we alter the test for non-reducing sugars?

A

we must hydrolyse them to break the bond. we can do this by adding H+ (an acid)

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12
Q

how is the structure of starch related to its function?

A

starch is INSOLUBLE so doesn’t affect OSMOSIS
it is a LARGE so doent’t DIFFUSE ot of cells
it HYDROLYSES to easily form ALPHA GLUCOSE for RESPIRATION
it is BRANCHED so can be RAPIDLY HYDROLYSED

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13
Q

how does the structure of glycogen differ to the structure of starch?

A

it is shorter and more highly branched

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14
Q

where is glycogen stored?

A

muscles

liver

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15
Q

how is the structure of glycogen related to it’s function?

A

starch is INSOLUBLE so doesn’t affect OSMOSIS
it is a LARGE so doent’t DIFFUSE ot of cells
it is more HIGHLY BRANCHED which means it can be rapidly HYDROLYSED for animals who have an incresed metabolic rate

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16
Q

what is the function of cellulose?

A

cellulose is in the cell walls and keeps the cell turgid

it also prevents osmotic lysis

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17
Q

<p>how is the structure of cellulose related to its function?</p>

A

<p>long unbranched chains are cross-linked increasing strength, the microfibrils form fibres (more strength) </p>

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18
Q

<p>what needs to happen for an enzyme to catalyse a reaction?</p>

A

<p>COLLISIONS to form an ESC</p>

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19
Q

<p>what is the molecular formula of glucose isomers?</p>

A

<p>C6H12O6</p>

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20
Q

<p>how can you overcome the effect of a competitive inhibitor?</p>

A

<p>increase substrate concentration </p>

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21
Q

what does a non competitive inhibitor do?

A

bind with another site
alter the tertiary structure
is not affected by substrate conc

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22
Q

what types of carbohydrate are glucose, galactose and fructose?

A

monosaccharides

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23
Q

what disaccharide do glucose and fructose make?

A

sucrose

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24
Q

what disaccharide do glucose and galactose make?

A

lactose

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25
what disaccharide do 2 x glucose make?
maltose
26
what bond is present in lipids?

ESTER BONDS

27

what are the differences between a triglyceride and a phospholipid

in a triglyceride one of the fatty acid groups is changed to a phosphate group

28
draw the structure of an amino acid
``` H R O \ | // N-C-C / | \ H H OH ```
29
describe the emulsion test
macerate then add ethanol, water shake
30
what are the 3 bonds in tertiary structure?
ionic, hydrogen, disulphide bridges
31
what are 3 useful properties of water?
cohesive, high surface tension, high latent heat of vaporisation
32
what bonds join nucleotides together in the sugar / phosphate backbone?
phosphodiester bonds
33
Describe how an ESC is formed.
The Tertiary structure of the active site is complementary to the shape of the substrate so forms an ESC
34
Describe how a mutation may cause a non functioning enzyme =.
Changed the primary structure changing the tertiary structure ---> change to the active site substrate is not complimentary no ESC formed
35
Describe how when a enzyme has denatured the ESC cannot form.
ionic bonds are changed altering the tertiary structure ----> active site the substrate is not complementary the ESC does not form
36
What does it mean when an enzyme has denatured?
There is a permanent change to the active site so no more ESC can form
37
How does temp. affect rate of reaction (enzyme)
increasing temperature causes the molecules to vibrate more increasing no. collisions inc. percentage of collisions with activation energy more ESCs formed
38
How can increasing temp. cause the enzyme to denature?
Molecules vibrate more until internal bonds break this changes the shape of the active site ESCs don't form
39
Why does enzyme activity decrease when you move away from the optimum pH?
OH- or H+ interact with the ionic bonds of the active site causing ESCs to not form
40
What is the affect of increasing Enzyme Concentration on an Enzyme catalysed reaction?
the rate increases because there are increased collisions between substrates and enzymes more ESCs formed id substrate runs out the conc. of enzyme cannot change rate
41
What is the affect of substrate conc. on the rate of an enzyme catalysed reaction?
as you increase sub conc. the rate increases bc there are more collisions more ESCs formed Once all the active sites are occupied the enzyme conc is the limiting factor
42
What is a competitive inhibitor
similar shape to substrate so binds to the active site, preventing the formation of an ESC The proportion of substrate to comp. inhibitor will affect to what degree the rate changes
43
What is a non competitive inhibitor?
bind to the enzyme not at active site and alter the tertiary structure of the active site This means no ESCs form not affected by conc
44
Define proteins
polymers built up of amino acids
45
Define Amino Acid
the monomer that makes up a protein
46
What are the 3 main groups in an AA molecule? (draw and check)
amine groups, variable R group and carboxyl group
47
What are the bonds between AA?
peptide bonds
48
What type of reaction is involved in the formation of a polypeptide?
condensation
49
The 4 types of protein (EATS)
enzyme, antibody/gen, transport,structural
50
what is the colour change for a positive Biuret test?
Blue ------> Purple
51
Define Primary structure of a protein
the sequence of AA
52
what bonds are present in the primary structure of proteins?
Peptide
53
What is the Secondary structure?
the chains of AA fold into regions with repeated patterns eg) alpha helix, beta pleated sheets
54
what bonds are present in the secondary structure?
peptide bonds, hydrogen bonds
55
what is the tertiary structure?
the final 3D shape Eg) enzyme
56
what bonds are present in tertiary structure?
peptide. hydrogen, disulphide bridges, ionic
57
what is the quaternary structure?
more than one polypeptide chain
58
What type of molecule is water?
polar molecule
59
Why is water a good solvent for ionic compounds?
- small charges of water add up to equal the charge of the ion - the ion can dissolve/ break free from it's partner
60
What is cohesion
water molecules stick together because to intermolecular H+ bonds
61
Why does water have a high latent heat of vaporisation?
because it requires a lot of energy to break H+ bonds between molecules (evaporation is therefore, an effective way of cooling down)
62
Why is water having a high specific heat capacity useful?
aquatic environments remain stable, temperature control of our bodies
63
What is an ion?
an atom that has lost or gained electrons (charged)
64
What are the 5 key ions to consider? (think why)
H+ ions, iron ions, calcium ions, sodium, phosphate

Biology Revision Year 1 (13 decks)

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