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foundations in biology > biological molecules > Flashcards

biological molecules Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What type of molecule is water?

A

polar

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2
Q

what is the strength of hydrogen bonds?

A

weak

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3
Q

water’s thermal properties

A
  • high SHC helps maintain optimum temp for enzyme activity
  • is a temp buffer for chemical reactions
  • ice is less dense than water (temp decrease = KE decrease so maximum number of bonds can form, and molecules spread out and form a lattice)
  • this means water under ice remains water and ice acts as an insulator
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4
Q

waters solvent properties

A
  • ions are attracted to water as it is polar
  • allows for the uptake of minerals by organisms
    eg. nitrate for amino acids or phosphate for ATP
  • dilute toxic solutions
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5
Q

water’s transport function

A
  • transpiration stream
  • transport dissolved metabolites
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6
Q

what is a condensation reaction?

A

two molecules combine and water is formed

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7
Q

what is hydrolysis?

A

water is added and one molecue splits into 2

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8
Q

what is the bond between two amino acids?

A

peptide bond

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9
Q

what is the primary structure of a protein?

A

the order of amino acids

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10
Q

what is the secondary structure of a protein?

A
  • folding of the peptide chain
  • alpha helix spirals and is held together with hydrogen bonds
  • beta pleated sheets fold into anti-parallel chains and each one is held with hydrogen bonds
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11
Q

what is the tertiary structure of proteins?

A

globular proteins fold into a 3D shape

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12
Q

how do R groups interact to determine tertiary structure?

A
  • disulfide bridges between cysteine
  • hydrogen bonds
  • ionic bonds between oppositely charged R groups
  • hydrophilic heads on outside to interact with water
  • hydrophobic tails on inside
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13
Q

what is the quaternary structure of a protein?

A

chains of polypeptides in a closely packed arrangement

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14
Q

what are globular proteins

A
  • soluble
  • round molecule
  • specific 3D shape
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15
Q

what three elements are carbohydrates made of?

A
  • carbon
  • hydrogen
  • oxygen
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16
Q

examples of monosaccharides

A
  • glucose
  • fructose
  • ribose
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17
Q

exampes of disaccharides

A
  • lactose
  • sucrose
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18
Q

examples of polysaccharides

A
  • glycogen
  • cellulose
  • starch
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19
Q

what are the two forms of glucose?

A

alpha and beta

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20
Q

difference between alpha and beta glucose

A

H-OH are flipped to OH on top on the left in beta

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21
Q

what is the bond in sucrose?

A

1-4 glycosidic

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22
Q

bond between glucose

A

1-4 glycosidic bonds

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23
Q

what is maltose made up of?

A

2 glucose

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24
Q

what is sucrose made up of?

A

glucose+fructose

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25
Q

what is lactose made up of?

A

galactose+glucose

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26
Q

what is the energy store in plants?

A

starch

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27
Q

what is the energy store in animals?

A

glycogen

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28
Q

what bonds do glycogen have?

A

1-6 glycosidic

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29
Q

why is the energy store in animals different to plants?

A

-glycogen is less dense and more soluble so can be broken down faster
- animals have higher metabolic demands

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30
Q

what is cellulose made of?

A

beta glucose and 1-4 glycosidic bonds

31
Q

what are the properties of cellulose that make it suitable for plant cell walls?

A
  • insoluble
  • unreactive
  • beta glucose
  • high tensile strength
  • flexible
32
Q

what are lipids soluble in?

A

ethanol

33
Q

bond between fatty acids and glycerol

A

ester bond

34
Q

structure of triglycerides

A
  • 3 glycerol+fatty acid tails
  • 3 ester bonds
35
Q

structure of phospholipids

A
  • hydrophilic heads and hydrophobic tails
  • 2 ester bonds
  • two fatty acids
36
Q

what is the role of lipids?

A
  • energy store
  • protection of organs
  • insulator
37
Q

what is the test for starch?

A

iodine (black=positive)

38
Q

what is the test for lipids?

A
  • ethanol (cloudy precipitate = positive)
  • add ethanol then water
39
Q

what is the test for proteins?

A

biurets (purple=positive)
- add copper sulfate solution and sodium hydroxide and biuret reagent

40
Q

what is the test for reducing sugars?

A

benedicts (green-red)
compare to known results to become qualitative

41
Q

what is the test for non-reducing sugars?

A
  • add HCl to hydrolyse solution
  • sucrose to glucose+fructose
  • heat solution in a boiling water bath
  • add benedicts solution
42
Q

what is the effect of cholesterol on phospholipids?

A

affects permeability and flexibility

43
Q

how do R groups interact to form tertiary structure?

A
  • oppositely charged R groups form strong ionic bonds
  • R groups with sulfer can form disulfide bonds
  • hydrophilic and hydrophobic interactions
  • hydrogen bonds with most other R groups
44
Q

how would you obtain amino acids from haemoglobin with RBC’s?

A

haemoglobin is hydrolysed and broken down by protease

45
Q

insulin

A
  • globular protein that regulates blood glucose
  • soluble yo be transported in blood
  • fits receptors on cell surface mebrane
46
Q

catalase

A
  • enzyme that increases ROR
  • globular protein with quaternary
  • iron II haem group binds to substrate (usually hydrogen peroxide) to speed up break down
47
Q

haemoglobin

A

-globular and prosthetic groups
- 2 alpha and 2 beta chains
- 4 groups
- iron ions reversibly binds with oxygen

48
Q

fibrous proteins

A
  • long and insoluble
  • lots of hydrophobic R groups
  • repetetive
49
Q

collagen

A
  • strong and flexible
  • three polypeptide chains wound around eachother to prevent snapping
  • formed from glyceine which is the smallest amino acid which allows for a tight configuration
50
Q

keratin

A
  • fibrous protein
  • lots of cysteine so disulfide bonds
  • number of bonds determines flexibility
51
Q

elastin

A
  • elastic fibres
  • can stretch and recoil easily
52
Q

what are the properties and functions of globular proteins?

A
  • specific 3D structure means they make up antibodies for immunity
  • hydrophilic exterior for transporting molecules (carrier/channel proteins)
  • conjugated to form receptors for cell signalling
  • 3D shape complementary to substrates to form enzymes as catalysts
53
Q

what are the properties and functions of fibrous proteins?

A
  • strong and tough to provide structure eg collagen around vessels
  • flexible due to elastic properties eg in vessel walls to stretch and recoil
  • elongated for the contraction and movement of cilia
54
Q

what is amylopectin?

A

highly branched chain of alpha glucose

55
Q

what bonds are in amylopectin?

A

both 1-4 and 1-6 glycosidic

56
Q

why is the structure of amylopectin important?

A

enzymes can easily access bonds to quickly break it down into glucose monomers

57
Q

what is amylose?

A

linear chain of alpha-glucose

58
Q

what bonds are in amylose?

A

1-4 glycosidic

59
Q

why is the structure of amylose important?

A

chains have a helical structure which allows for tight packing, hence useful for storage

60
Q

what is the difference between glycogen and amylopectin?

A
  • glycogen is the primary storage form of glucose in animals, while amylopectin is the primary storage form of glucose in plants
  • glycogen is more soluble than amylopectin, which is insoluble in water
  • glycogen has more branches than amylopectin, which makes it more compact and efficient
  • glycogen has more α-1,6-glycosidic bonds than amylopectin, which has more α-1,4-glycosidic bonds
61
Q

what are the differences bewteen glycogen and cellulose?

A
  • glycogen is branched and forms coils whereas cellulose forms straight chains
  • glycogen has 1-4 and 1-6 whereas cellulose has 1-4
  • glycogen is alpha and cellulose is beta
62
Q

how does glycogen act as an energy source?

A
  • glycogen can be hydrolysed to glucose.
  • the glucose could then be used to release energy through the process of respiration
63
Q

how is starch adapted to its function in the cells of plants?

A
  • insoluble in water so doesnt affect the cells water potential
  • helical shape so can be closely stored
  • large so unable to leave the cell
64
Q

why do mammals store glycogen instead of glucose?

A
  • insoluble so no effect on water potential
  • metabolically inactive
  • compact so can store lots of energy in a smaller space
  • highly branched so can hydrolyse to glucose when needed
65
Q

why is collagen is a fibrous protein?

A
  • long chain of amino acids
  • no tertiary structure
  • insoluble
66
Q

why is collagen so strong?

A

many covalent and hydrogen bonds

67
Q

outline the method of chromatography that will separate the main amino acids in collagen

A
  • hydrolyse collagen into amino acids
  • place sample on chromatography paper
  • dry and repeat
  • place paper in solvent (ethanoic acid)
68
Q

what are some ways in which the molecular structure of cholesterol is similar to the molecular
structure of glucose?

A
  • both have C and H atoms
  • both contain oxygen
  • both have a hydroxyl group
69
Q

why can glucose be transported in the bloodstream?

A

soluble in water

70
Q

how could you improve a chromatography method?

A
  • wear gloves to prevent transfer of amino acids from hands
  • put pencil and amino acids higher than solvent line to prevent them mixing
  • put a cover over beaker to prevent evaporation
  • repeat and find a mean to improve accuracy
  • label amino acid samples to prevent confusion
71
Q

what is esterification?

A
  • reaction between fatty acids and glycerol
  • condensation reaction
72
Q

how does the structure of glycogen differs from that of amylopectin to make it better suited as an energy store in animals?

A
  • glycogen is more branched and coiled
  • more compact
  • free ends to easily add or remove glucose when needed
73
Q

how is chitin formed from its monomers and predict its structure

A
  • glycosidic bonds formed by a condensation reaction where a water molecule is released
  • forms a linear glucose chain similar to cellulose
74
Q

what is meant by the term conjugated protein

A
  • contains non protein groups
  • has prosthetic group of iron which is attached by hydrogen bonds

foundations in biology (6 decks)

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