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Biology Y12 > Biological molecules > Flashcards

Biological molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

what is metabolism?

A

the total sum/rate of all chemical reactions within an organism

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2
Q

what are the two types of metabolism?

A

catabolic: larger complex molecules broken to smaller
C - the break down of substances releasing energy

anabolic: smaller molecules built to larger molecules
A - the synthesis of substances requiring energy

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3
Q

what are organic molecules?

A

contain carbon and hydrogen

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4
Q

what are monomers?

A

are small repeating units which join together to form larger molecules

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5
Q

what are polymers?

A

large molecules made up small repeating units called monomers

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6
Q

carbohydrate monomers + polymers?

A

monomers: monosaccharies
polymers: polysaccharides

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7
Q

proteins monomer + polymers?

A

monomer: amino acids
polymer: polypeptides/proteins

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8
Q

nucleic acid monomer + polymers?

A

monomers: nucleotides
polymers: dna/rna

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9
Q

what is a condensation reaction

A

joins to molecules together with the formation of a chemical bond and involves the elimination of water

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10
Q

what is a hydrolysis reaction?

A

breaks a chemical bond between 2 molecules involving the use of a water molecule

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11
Q

what is a carbohydrate?

A

a molecule that contains carbon,hydrogen and oxygen with the ratio 1:2:1

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12
Q

function of carbohydrates?

A

provide energy/important source of energy for plants and animals

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13
Q

what are the 3 main groups of carbohydrates

A

monsaccarides, disaccarides, polysaccarides

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14
Q

properties of monosaccharides?

A

water soluble, sweet tasting and form crystals

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15
Q

3 monosaccharides i need to know..?

A

glucose, fructose, galactose

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16
Q

which two monosaccharides make maltose?
where are the disaccharides found?

A

glucose + glucose 2.in malt sugar

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17
Q

which two monosaccharides make up sucrose?
where are the disaccharides found?

A

glucos + fructose 2.cane sugar

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18
Q

which two monosaccharides make up lactose
where are the disacchardies found?

A

glucose + galactose 2. milk sugar

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19
Q

draw and explain the difference between alpha and beta glucose

A

in alpha glucose the fist carbon has h on top oh on bottom whereas in beta glucose its switched

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20
Q

what type of molecules are Alpha and beta glucose?

A

Structural isomers

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21
Q

do monosaccharides need changing to be used in respiration?

A

they require little to no change

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22
Q

what is the general formula for monosaccharides?

A

CnH2n0

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23
Q

what is the general formula for disaccharides?

A

CnH2n-10n-1

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24
Q

if the number of carbon atoms is 3, 5, 6 the monosaccharide is called?

A

3= triose- glyceraldehyde
5=pentose - ribose
6=hexose - glucose, galactose

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25
Q

uses of monosaccharides?

A

building blocks and energy

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26
Q

biological role of monosaccharides as an energy source?

A

as an energy source a large amount of energy is stored between c-h bonds. this is released to form ATP. ATP is the energy currency of the cell.

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27
Q

biological role of monosaccharides as a building block?

A

repeated glucose molecules build up to form molecules such as starch and glycogen

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28
Q

what needs to happen to disaccharides before being used as energy?

A

need to be digested before they can be sued to release energy. Sugars are often in this form.

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29
Q

which one of the three main groups of carbohydrates are not sugars?

A

polysaccharides

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30
Q

give 3 examples of disaccharides

A

sucrose, lactose and maltose

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31
Q

what monomer is starch made up of?

A

alpha glucose

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32
Q

type of glycosidic bond?

A

amylose = 1-4 , amylopectin = 1-4 and 1-6 glycosidic bond

33
Q

describe the main structure of the starch chain?

A

helical chain

34
Q

what are the two forms of starch

A

amylose and amylopectin

35
Q

describe the structure of amylose a form of starch?

A

straight chain, no branches forms coil/spiral structure

36
Q

describe the structure of amylopectin another form of starch?

A

straight chain, branches at regular intervals formed by condensation

37
Q
  1. what is the average size of a starch polysaccharide?
  2. reducing or non-reducing?
  3. solubility in water?
  4. found in..?
    5 .molecule type?
A
  1. 1um-100um
  2. non-reducing
  3. insoluble
  4. plant cells
    straight chain polysaccharide
38
Q

explain the use of starch being insoluble?

A

doesn’t affect the water potential so water is not drawn out of cells by osmosis

39
Q

explain the use of starch being large and insoluble?

A

does not diffuse out of cells

40
Q

explain the use of starch beng coiled and compact?

A

can be stored in a small space

41
Q

when starch is hydrolysed it forms..?
explain why this is useful?

A

alpha glucose. alpha glucose is easily tranpsorted and readily used in respiration

42
Q

explain the use of starch having many branched ends

A

each branch can be acted on by enzymes, simultaeneously meaning that glucose monomers are released rapidly

43
Q

what monomers is glycogen made up of?

A

alpha glucose

44
Q

type of glycosidic bond?

A

1,6 - 1,4- glycosidic bond

45
Q

main structure of glycogen?

A

very branched structure, provide more sites for glucose to be released fast

46
Q
  1. relative size of glygogen molecule?
  2. type of molecule?
  3. reducing or non-reducing?
  4. solubility in water
A
  1. 20-30um
  2. branched polysaccharide
  3. reducing
  4. partially soluble
47
Q

why is glycogen insoluble

A

doesn’t tend to be drawn into cells by osmosis (doesn’t affect the water potential and does not diffuse out of cells)

48
Q

why is glycogen compact

A

large amount of energy can be stored in a small space

49
Q

why is glycogen highly branched

A

more ends can be acted on by enzymes simultaeneously more rapid break down to form glucose monomers for respiration

50
Q

what monomers is cellulose made from?

A

beta glucose

51
Q

type of glycosidic bond?

A

1,4 glycosidic bond

52
Q

main structure?

A

linear structure

53
Q
  1. size of molecule
  2. type of molecule?
  3. reducing or non-reducing?
  4. solubility in water?
A
  1. 2-10nm
  2. straight chain polysaccharide
  3. non-reducing
    4.insoluble
54
Q

explain how cellulose molecules are adapted to their function?

A
  • inward prsssure prevents cells from bursting as water enters by osmosis -?
  • long straight unbranched chains of many glucose molecules to strengthen cell wall
  • forms many firm hydrogen bonds between individual chains in cellulose microfibrils = strengthing effect
  • cellulose molecules are grouped to form microfibrills and microfibrils that are grouped form fibres providing more strength
55
Q

describe the test for starch?

A

add a few drops of iodine solution. positive result = blue/black neg result= yellow/brown

56
Q

describe the test for protein?

A

using biuret solution = sodium hydroxide and a few drops of copper sulphate. positive result = purple/lilac
neg result = blue

57
Q

describe the test for lipids

A

add ethanol to test sample and shake, add equal amounts of water. positive result = white emulsion is formed neg= clear

58
Q

all monosaccharides and some disaccharides are…?

A

reducing sugars

59
Q

What is a reducing suar?

A

a reducing sugar is a sugar that can donate electrons (reduce) another chemical

60
Q

describe the test for reducing sugar?

A

heat (water bath) test sample with benedicts solution. positive result = orange-red precipitate
neg result = blue/green

61
Q

why is Benedicts test semi-quantitative?

A

when heated with benedicts some solutions give different colours e.g brown, yellow, green, red. the differences in colour mean that it can be used to estimate the approximate amount of reducing sugar in a sample.
green = very low amount
yellow = low
brown = medium
red - high

62
Q

some disaccharides are..?

A

Non-reducing sugars

63
Q

describe the test for non- reducing sugar

A
  1. reducing sugar test
  2. boil solution with HCL to hydrolyse the glycosidic bond
  3. neutralise with sodium hydrogen carnonate
  4. heat with benedicts
    positive result - green–> orange-red precipitate
    negative result- no colour change
64
Q

what is the result for a reducing and non-reducing?

A

more intensely coloured precipitate deep orange-red

65
Q

what is the function of proteins?

A

providing structure, regulating body processes, transporting materials, balancing fluids, helping with immunity, and providing energy.

66
Q

draw and explain the structure of an amino acid?

A

amine group, carboxylic group and r-group

67
Q

how many types of amino acids are there?

A

20 different types so twenty different r groups

68
Q

what properties does the r group decide?

A

if the molecule is hydrophobic, hydrophillic, positively, negatively charged

69
Q
  1. where do plants get their protein from?
  2. how do animals get their protein?
  3. why cant access amino acids be stored in animals?
A
  1. nitrates from the soil
  2. from plants-digest-proteins-amino acids
  3. leads to toxicity deamination. deamination is the removal of amino acids. amino groups converted into urea and removed in urine.
70
Q

four levels of structure in a protein
1. primary structure - what is it determined by?
2. what does the sequence of amino acids determine?

A
  1. protein sequencing happens here . it is determined by a gene that codes for a polypeptide and a peptide bond forms.
  2. determines the properties and functions of that protein
71
Q
  1. . secondary structure- explain?
  2. folds into right handed alpha felix?
  3. this means that..?
A
  1. folding of the polypeptide chain
  2. the polypeptide would for a coil/helix structure, hydrogen bonds run parallel along the long helical axis
  3. it has a strong stable structure due to many hydrogen bonds
72
Q
  1. secondary structure
    - also folds into a beta pleated sheet?
A
  1. which folds back on its self forming a zigzag sheet, held together by hydrogen bonds
73
Q
  1. tiertiary structure - explain
    - the bonds which hold the tiertiary structure are?
A

final 3D shape where helixes and pleates are twisted and folded again
- disulphide - fairly strong, not easily broken
-ionic - between oppositly charged r groups, strong but weaker than disulphide bonds, not easily broken by chnages in ph
-hydrogen- between slightly oppositely charged groups, easily broken

74
Q
  1. what happens if the structure is heated?
  2. what happens if kinetic energy increases?
  3. why are most bonds weak?
A
  1. starts to unravel and starts to denature so can not function anymore
  2. molecules vibrate and breaks some bond holding structure
  3. because most bonds are not covalent
75
Q

what else happens at tiertiary structure?

A

forms globular or fibrous proteins

76
Q

what are globular proteins?

A

roll into a compact globe/ball shaped structure,
hydrophobic inward, hydrophillic outward,
are enzymes, plasm proteins and antibodies, have metabolic roles

77
Q

what re fibrous proteins?

A

form fibres, regular/repetitive sequences of amino acids,
usually insoluble in water
have structural roles

78
Q

what is quaternity structure of a protein?

A

made up of multiple polypeptide chains

79
Q

FINISH

A

Biology Y12 (20 decks)

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