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A-Level Biology > Unit 1 > Flashcards

Unit 1 Flashcards

Biological Molecules

1
Q

define polymer

A

molecules formed when multiple monomers are joined together

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2
Q

define monomer

A

smaller, basic units that join together to form larger molecules

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3
Q

what happens in a condensation reaction?

A

formation of a chemical bond between two molecules involving the elimination of a water molecule

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4
Q

what happens in a hydrolysis reaction?

A

breaking of a chemical bond between two molecules through the use of a water molecule

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5
Q

give three examples of monomers

A

monosaccharides, amino acids, nucleotides

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6
Q

name the three monosaccharides

A

glucose, galactose, fructose

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7
Q

name the bond that forms between two monosaccharides

A

glycosidic bonds

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8
Q

give the molecular formula of a monosaccharide

A

C6H12O6

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9
Q

what elements are in carbohydrates?

A

C, H, O

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10
Q

name three disaccharide’s

A

Maltose, sucrose, lactose

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11
Q

Maltose is formed in the condensation reaction between…

A

two (Alpha) Glucose

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12
Q

Sucrose is formed in the condensation reaction between…

A

(Alpha) Glucose and fructose

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13
Q

Lactose is formed in the condensation reaction between…

A

(Alpha) Glucose and galactose

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14
Q

describe the difference between between alpha and beta glucose

A

hydroxyl group is reversed (alpha has OH on the bottom of the right side)

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15
Q

give the molecular formula of a disaccharide

A

C12H22O11

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16
Q

what storage molecule do plants use

A

starch (some glycogen)

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17
Q

what storage molecule do animals use

A

glycogen

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18
Q

what are the two types of starch

A

amylose and amylopectin

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19
Q

give three properties that make starch useful

A

insoluble - no effect on water potential
large - doesn’t diffuse out of the cell
branched - quick hydrolysis of glucose

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20
Q

describe the structure (and function) of amylose

A

alpha-helix shape with hydrogen bonds between (makes it compact), 1-4 glycosidic bonds (no branching)

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21
Q

describe the structure (and function) of amylopectin

A

branched (many terminal ends for the hydrolysis of glucose), 1-4 and 1-6 glycosidic bonds (alpha glucose)

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22
Q

describe the structure (and function) of glycogen

A

branched (many terminal ends for the hydrolysis of glucose), 1-4 and 1-6 glycosidic bonds (alpha glucose)

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23
Q

describe the structure of cellulose

A

1-4 glycosidic bonds between beta glucose forming straight chains, microfibrils are formed due to hydrogen bonds

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24
Q

what is the test for reducing sugars

A

Benedict’s reagent, heat in water bath, positive result; blue to green to brick red

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25
what is the test for non-reducing sugars (sucrose)
heat and acid (HCl), then the Benedict's test
26
what is the test for starch
iodine, positive result; brown to black
27
difference between saturated and unsaturated fats
unsaturated have double C-C bonds
28
why are unsaturated lipids liquid at room temperature
double bonds mean unsaturated can bend and cannot become compact
29
what does a triglyceride consist of
1 glycerol and 3 fatty acids
30
what does a phospholipid consist of
1 phosphate group, 1 glycerol and 2 fatty acids
31
what is the name of the bond between glycerol and fatty acids
ester bond
32
why can phospholipids form a bilayer/micelles
they have a hydrophilic (polar) head and hydrophobic (non-polar) tails
33
describe the emulsions test
shake with ethanol, add water, positive result; cloudy-white colour
34
give the structural formula of an amino acid
NH2CH(R)COOH
35
what are different amino acids defined by
the R group
36
how many amino acids are there
20
37
name the bond between amino acids
peptide bond
38
whats the difference between a dipeptide and polypeptide
di is 2 and poly is more than
39
describe the primary structure
the sequence of amino acids (peptide bonds)
40
describe the secondary structure
either a beta-pleated sheet or alpha-helix (hydrogen bonds)
41
describe the tertiary structure
folded into a 3D shape (hydrogen, ionic, disulfide)
42
describe the quaternary structure
multiple polypeptides (sometimes with a prosthetic group)
43
what is the difference between a fibrous and globular protein
globular are usually compact and have a purpose, fibrous are repeating units (mutation is less likely) that form fibers
44
describe the biuret test
add biuret solution, positive result; blue to purple
45
describe an enzyme
biological catalyst that lowers activation energy, 3D tertiary globular structure
46
describe the induced fit model
the enzyme binds the the complementary substrate, forming an enzyme-substate-complex. the active site alters to fit the substrate
47
whats the main difference between the 'lock and key' and 'induced fit'
in the 'lock and key' the enzyme and substrate are the exact same shape
48
effect of temperature on enzyme action
rate of reaction increases as kinetic energy is increased, collision is more likely (more enzyme-substrate-complexes) after optimum hydrogen bonds break and the enzyme denatures (less enzyme-substrate-complexes)
49
effect of pH on enzyme action
as pH moves away from optimum H+ and OH- cause the ionic bonds to break and the enzyme to denature (less enzyme-substrate-complexes)
50
effect of enzyme concentration on enzyme action
originally increases (more enzyme-substrate-complexes) until substrate become a limiting factor and rate of reaction plateaus (less enzyme-substrate-complexes)
51
effect of substrate concentration on enzyme action
originally increases (more enzyme-substrate-complexes) until active sites are filled and rate of reaction plateaus (less enzyme-substrate-complexes)
52
describe a competitive inhibitor
binds to active site so enzyme-substrate-complexes can't form
53
describe a non-competitive inhibitor
binds to the allosteric site and alters the enzymes active site so enzyme-substrate-complexes can't form
54
what type of replication is in DNA
semi-conservative replication
55
describe DNA replication
DNA helicase breaks hydrogen bonds between complementary bases, complementary nucleotides are joined to the template strand by DNA polymerase, 2 identical strands form
56
describe the structure of a nucleotide
phosphate, pentose sugar and a nitrogenous base (adenine, thymine, cytosine, and guanine)
57
describe the structure of ATP
adenine, ribose sugar, 3 phosphate groups
58
properties of ATP
small amounts of energy released at a time, easily resynthesised by ADP and Pi
59
give properties of water
used in metabolic reactions, solvant, polar, high specific heat capacity and water of vaporisation
60
purpose of phosphate ions
in ATP, RNA, DNA
61
purpose of Fe
prosthetic group of haemoglobin, carries oxygen

A-Level Biology (9 decks)

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